Vitrified Specimens
Complete List


Bacterial Flagella and Basal Body Complex

Trachtenberg, S., D. Stokes, E. Bullitt and D. DeRosier (1986) Actin and flagellar filaments: Two helical structures with variable twist. Annals of the New York Academy of Sciences: Recent Advances in Electron and Light Optical imaging in biology and Medicine 483:88-99.

Trachtenberg, S. and D. J. DeRosier (1988) Three-dimensional reconstruction of the flagellar filament of Caulobacter crescentus. A flagellin lacking the outer domain and its amino acid sequence lacking an internal segment. J. Mol. Biol. 202:787-808.

Sosinsky, G. E., N. R. Francis, M. J. B. Stallmeyer and D. J. DeRosier (1992) Substructure of the flagellar basal body of Salmonella typhimurium. J. Mol. Biol. 223:171-184.

Trachtenberg, S. and D. J. DeRosier (1992) Conformational switching in the flagella filament of Salmonella typhimurium. J. Mol. Biol. 226:447-454.

Trachtenberg, S., K. R. Leonard and W. Tichelaar (1992) Radial mass density functions of vitrified helical specimens determined by scanning transmission electron microscopy: their potential use as substitutes for equatorial data. Ultramicroscopy 45:307-321.

Ruiz, T., N. R. Francis, D. G. Morgan and D. J. DeRosier (1993) Size of the export channel in the flagellar filament of Salmonella typhimurium. Ultramicrosc. 49:417-425.

Francis, N. R., G. E. Sosinsky, D. Thomas and D. J. DeRosier (1994) Isolation, characterization and structure of bacterial flagellar motors containing the switch complex. J. Mol. Biol. 235:1261-1270.

Morgan, D. G., C. Owen, L. A. Melanson and D. J. DeRosier (1995) Structure of bacterial flagellar filaments at 11Å resolution: Packing of the a-helices. J. Mol. Biol. 249:88-110.

Meeting Abstracts, Newsletters and Bulletins

Sosinsky, G. E., N. R. Francis, C. D. DeRosier, D. J. DeRosier, J. Hainfeld and J. Wall (1990). The structure and subunit organization of the bacterial flagellar motor by scanning transmission electron microscopy and cryoelectron microscopy. Proc. XII Int'l. Cong. Elec. Microsc. (Seattle) 1:278-279.

Francis, N. R., G. E. Sosinsky, D. Thomas and D. J. DeRosier (1992) Three-Dimensional Reconstruction of the Bacterial Basal Body/Switch Complex by Electron Cryomicroscopy. Proc. Elect. Microsc. Soc. Am. 50:514-515.

Morgan, D. G., C. Owen, L. Melanson and D. J. DeRosier (1992) New Methods for the Analysis of Helical Objects: Application of Cross-Correlation Techniques. Proc. Elect. Microsc. Soc. Am. 50:516-517.

Ruiz, T., R. Diaz, J.-L. Ranck, D. L. D. Caspar and D. J. DeRosier (1992) Electron Diffraction of Helical Structures. Proc. Elect. Microsc. Soc. Am. 50:518-519.

Trachtenberg, S. and D. J. DeRosier (1992) Conformational Switching in the Flagellar Filament of Salmonella typhimurium. Proc. Elect. Microsc. Soc. Am. 50:538-539.

Trachtenberg, S., K. R. Leonard and W. Tichelaar (1992) Linear and Radial Mass Density of Vitrified Helical Specimens Determined by Scanning Transmission Electron Microscopy. Proc. Elect. Microsc. Soc. Am. 50:534-535.



Chaperonins

Hutchinson, E. G., W. Tichelaar, G. Hofhaus, H. Weiss and K. R. Leonard (1989) Identification and electron microscopic analysis of a chaperonin oligomer from Neurospora crassa mitochondria. EMBO J.. 8:1485-1490.



Clathrin

Vigers, G. P. A., R. A. Crowther and B. M. F. Pearse (1986) Three-dimensional structure of clathrin cages in ice. EMBO J. 5:529-534.

Vigers, G. P. A., R. A. Crowther and B. M. F. Pearse (1986) Location of the 100 kd-50kd accessory proteins in clathrin coats. EMBO J. 5:2079-2085.



Cryo-Sections

Sjostrom, M. and J. M. Squire (1977) Cryo-ultramicrotomy and myofibrillar fine structure: a review. J. Microsc. 111:239-278.

Sjostrom, M. and J. M. Squire (1977) Fine structure of the a-band in cryo-sections: the structure of the a-band of human skeletal muscle fibres from ultra-thin cryo-sections negatively stained. J. Mol. Biol. 109:49-68.

Squire, J. M., J. J. Harford, A. C. Edman and M. Sjostrom (1982) Fine structure of the a-band in cryo-sections. J. Mol. Biol. 155:467-494.

Chang, J.-J., A. W. McDowall, J. Lepault, R. Freeman, Walter, C. A. and J. Dubochet (1983) Freezing, sectioning and observation artefacts of frozen hydrated sections for electron microscopy. J. Microsc. 132:109-123.

McDowall, A. W., J.-J. Chang, R. Freeman, J. Lepault, Walter, C. A. and J. Dubochet (1983) Electron microscopy of frozen hydrated sections of vitreous ice and vitrified biological samples. J. Microsc. 131:1-9.

Meeting Abstracts, Newsletters and Bulletins

Squire, J. M., M. Sjostrom and P. Luther (1976) Fine structure of the A-band in cryo-sections. II. Evidence for a length-determining protein in the thick filaments of vertebrate skeletal muscle. Sixth Europ. Reg. Conf. Elec. Microsc. (Jerusalem) 2:91-95.

Chang, J.-J., A. W. McDowall, C. A. Walter, R. Freeman, , J. Lepault and J. Dubochet (1982) Frozen hydrated sections of biological material. Proc. Tenth Int'l. Cong. Elec. Microsc. (Hamburg) 3:117-118.

Richter, K. and J. Dubochet (1990). High-resolution study of DNA in vitrified sections. Proc. XII Int'l. Cong. Elec. Microsc. (Seattle) 1:488-489.

Sjostrand, F. S. (1990) Common sense in electron microscopy about cryofixation, freeze-substitution, low temperature embedding, and low denaturation embedding. J. Struct. Biol. 103:135-139.

Richter, K., H. Gnagi and J. Dubochet (1991) A model for cryosectioning based on the morphology of vitrified ultrathin sections. J. Microsc. 163:19-28.

Sabanay, I., T. Arad, S. Weiner and B. Geiger (1991) Study of vitrified, unstained frozen tissue sections by cryoimmunoelectron microscopy. J. Cell Sci. 100:227-236.

Michel, M., T. Hillmann and M. Muller (1991) Cryosectioning of plant material frozen at high pressure. J. Microsc. 163:3-18.

Quintana, C. (1994) Cryofixation, cryosubstitution, cryoembedding for ultrastructural, immunocytochemical and microanalytical studies. Micron 25:63-99.



Chromatin and Chromosomes

Dubochet, J., M. Adrian, P. Schultz and P. Oudet (1986) Cryo-electron microscopy of vitrified SV40 minichromosomes: the liquid drop method. EMBO J.. 5:519-528.

McDowall, A. W., J. M. Smith and J. Dubochet (1986) Cryo-electron microscopy of vitrified chromosomes in situ. EMBO J. 5:1395-1402.

Meeting Abstracts, Newsletters and Bulletins

Athey, B., J. Langmore, S. Williams, M. Smith, C. F. Chang, R. Grant and W. Chiu (1987) Cryo-electron microscopy of chromosome fibers is consistent with the crossed-linker model for chromatin structure. Proc. Elec. Microsc. Soc. Am. 45:648-649.

Langmore, J. P., M. F. Smith and D. A. Rankert (1990). Quantitative energy-filtered cryo-EM of hydrated chromosome fibers, viruses, and heavy atoms. Proc. XII Int'l. Cong. Elec. Microsc. (Seattle) 1:252-253.



DNA

Downing, K. H. and R. M. Glaeser (1980) Electron diffraction from single crystals of DNA. Biophys. J. 32:851-856.

Lepault, J., J. Dubochet, W. Baschong and E. Kellenberger (1987) Organization of double-stranded DNA in bacteriophages: A study by cryo-electron microscopy of vitrified samples. EMBO J. 6:1507-1512.

Dustin, I., P. Furrer, A. Stasiak, J. Dubochet, J. Langowski and E. Egelman (1991) Spatial visualization of DNA in solution. J. Struct. Biol. 107:15-21.

Bednar, J., P. Furrer, A. Stasiak, J. Dubochet, E. H. Egelman and A. D. Bates (1994) The twist, writhe and overall shape of supercoiled DNA change during counterion-induced transition from a loosely to tightly interwound superhelix: possible implication for DNA structure in vivo. J. Mol. Biol. 235:825-847.

Meeting Abstracts, Newsletters and Bulletins

Downing, K. H. (1983) Electron crystallographic studies of DNA structure. Proc. Elec. Microsc. Soc. Am. 41:434-435.

Richter, K. and J. Dubochet (1990). High-resolution study of DNA in vitrified sections. Proc. XII Int'l. Cong. Elec. Microsc. (Seattle) 1:488-489.

Bednar, J., P. Furrer, A. Stasiak and J. Dubochet (1991) Cryo-electron microscopy: The method of choice for direct study of 3D-shape of individual DNA molecules in solution. Proc. Elect. Microsc. Soc. Am. 50:590-591.



DNA-Protein Complexes and
DNA-Binding Proteins

DNA Helix Destabilizing Protein

Cohen, H. A., W. Chiu and J. Hosoda (1983) Electron microscopy of T4 DNA helix destabilizing protein (gp32*i) crystal. Elec. Microsc. Soc. Am. Proc. 41:728-729.

Grant, R. A., M. F. Schmidt, W. Chiu, J. F. Deatherage, and J. Hosoda (1984) Alignment and merging of electron microscope images of frozen hydrated crystals of the T4 DNA helix destabilizing protein. Biophys. J. 49:251-258.

Grant, R. A., M. F. Schmid, W. Chiu, J. F. Deatherage, and J. Hosoda (1986) Alignment and merging of electron microscope images of frozen hydrated crystals of the T4 DNA helix destabilizing protein gp32*I. Biophys. J. 49:251-258.

Soejima, T., M. B. Sherman, M. F. Schmid and W. Chiu (1993) 4Å projection map of bacteriophage T4 DNA helix- destabilizing protein (gp32*I) crystal by 400-kV electron cryomicroscopy. J. Struct. Biol. 111:9-16.

RecA

Chang, C.-F., D. A. Rankert, T.-W. Jeng, D. G. Morgan, M. F. Schmid and W. Chiu (1988) Cryo electron microscopy of unstained, unfixed RecA-cssDNA complexes. J. Ultrastruc. Mol. Struct. Res. 100:166-172.

Egelman, E. H. and A. Stasiak (1993) Electron microscopy of RecA-DNA complexes: Two different states, their functional significance and relation to the solved crystal structure. Micron 24:309-324.

Ogawa, T., X. Yu, A. Shinohara and E. H. Egelman (1993) Similarity of the yeast RAD51 filament to the bacterial RecA filament. Science 259:1896-1899.

Egelman, E. H. and X. Yu (1992) DNA complexed with RecA protein. Proc. Elect. Microsc. Soc. Am. 50:448-449.

Other

Gogol, E. P., M. C. Young, W. L. Kubasek, T. C. Jarvis and P. H. vonHipple (1990). T4 replication accessory proteins visualized as complexes with DNA by cryoelectron microscopy. Proc. XII Int'l. Cong. Elec. Microsc. (Seattle) 1:264-265.

Gogol, E. P., M. C. Young and P. H. v. Hippel (1992) Transient DNA-protein complexes trapped and studied by cryoelectron microscopy. Proc. Elect. Microsc. Soc. Am. 50:446-447.


Enzymes

a2 Macroglobulin

Stoops, J. K., J. P. Schroeter, J.-P. Bretaudiere, N. Olson, H., T. S. Baker and D. K. Strickland (1991) Structural studies of human a2 macroglobulin: Concordance between projected views obtained by negative-stain and cryoelectron microscopy. J. Struc. Biol. 106:172-178.

Boisset, N., R. Grassucci, P. Penczak, E. Delain, F. Pochon, J. Frank and J. N. Lamy (1992) Three-dimensional reconstruction of a complex of human a2 macroglobulin with monomaleimido nanogold (Au 1. 4nm) embedded in ice. J. Struct. Biol. 109:39-45.

Delain, E., F. Pochon, M. Barray and F. v. Leuven (1992) Ultrastructure of a2 -macroglobulins. Elect. Microsc. Rev. 5:231-281.

Schroeter, J. P., S. J. Kolodziej, T. Wagenknecht, J.-P. Bretaudiere, J. T. Bretaudiere, D. K. Strickland and J. K. Stoops (1992) Three-dimensional structures of the human a2-macroglobulin-methylamine and chymotryrpsin complexes. J. Struct. Biol. 109:235-247.

Boisset, N., P. Penczek, F. Pochon, J. Frank and J. Lamy (1993) Three-dimensional architecture of human a2- macroglobulin transformed with methylamine. J. Mol. Biol. 232:522-529.

Catalase

Taylor, K. A. and R. M. Glaeser (1974) Electron diffraction of frozen, hydrated protein crystals. Science 186:1036-1037.

Taylor, K. A. and R. M. Glaeser (1976) Electron microscopy of frozen hydrated biological specimens. J. Ultrast. Res. 55:448-456.

Taylor, K. A. (1978) Structure determination of frozen, hydrated, crystalline biological specimens. J. Microsc. 112:115-125.

Fatty Acid Synthase

Stoops, J. K., S. J. Kolodziej, J. P. Schroeter, J. P. Bretaudiere and S. J. Wakil (1992) Structure-function relationships of the yeast fatty acid synthase: negative-stain, cryo-electron microscopy, and image analysis studies of the end views of the structure. Proc. Nat. Acad. Sci. USA 89:6585-6589.

Pyruvate Dehydrogenase Complex

Grassucci, R. A., T. Wagenknecht, G. A. Radke and T. E. Roche (1990). Cryoelectron microscopy of frozen-hydrated pyruvate dehydrogenase complexes. Proc. XII Int'l. Cong. Elec. Microsc. (Seattle) 1:260-261.

Wagenknecht, T., R. Grassucci and D. Schaak (1990) Cryoelectron microscopy of frozen-hydrated a-ketoacid dehydrogenase complexes from Escherichia coli. J. Biol. Chem. 265:22402-22408.

Stoops, J. K., T. S. Baker, J. P. Schroeter, S. J. Kolodziez, , X.-D. Niu and L. J. Reed (1992) Three-dimensional structure of the truncated core of the saccharomyces cerevisiae pyruvate dehydrogenase complex determined from negative stain and cryoelectron microscopy images. J. Biol. Chem. 267:24769-24775.

Wagenknecht, T., R. Grassucci, J. Berkowitz and C. Forneris (1992) Configuration of interdomain linkers in pyruvate dehydrogenase complex of Escherichia coli as determined by cryoelectron microscopy. J. Struct. Biol. 109:70-77.

Ubiquinone Oxidoreductase

Brink, J., F. P. Booy and F. J. Van Bruggen (1989) Computer image analysis of two-dimensional crystals of beef heart NADH: Ubiquinone oxidoreductase fragments: II. Comparison of frozen hydrated and negatively stained specimens. Ultramicrosc. 27:91-100.



Eukaryotic Flagella

Murray, J. M. (1986). Studies of eukaryotic flagella by cryoelectron microscopy. Annals of the New York Academy of Science: Recent Advances in Electron and Light Optical imaging in biology and Medicine Ed. A. P. Somlyo. New York, The N.Y. Academy of Sciences.



Immunoglobulins

Grant, R. A., L. L. Degn, W. Chiu and J. Robinson (1983) Electron microscopy of rabbit Fc crystals. Elec. Microsc. Soc. Am. Proc. 41:730-731.

Wade, R. H., J. C. Taveau and J. N. Lamy (1989) Concerning the axial rotational flexibility of the Fab regions of immunoglobulin G. J. Mol. Biol. 206:349-356.



Membranes

Acetylcholine Receptor

Brisson, A. and P. N. T. Unwin (1985) Quaternary structure of the acetylcholine receptor. Nature 315:474-477.

Toyoshima, C. (1990). Three-dimensional image analysis of tubular crystals of membrane proteins in ice. Proc. XII Int'l. Cong. Elec. Microsc. (Seattle) 1:242-243.

Toyoshima, C. and N. Unwin (1990) Three-dimensional structure of the acetylcholine receptor by cryoelectron microscopy and helical image reconstruction. J. Cell Biol. 111:2623-2635.

Unwin, N. (1993) Nicotinic acetylcholine receptor at 9A resolution. J. Mol. Biol. 229:1101-1124.

ATPases

Franzini-Armstrong, C., D. G. Ferguson, L. Castellani and L. Kenney (1986). The density and disposition of Ca-ATPase in IN SITU and isolated sarcoplasmic reticulum. Annals of the New York Academy of Sciences: Recent Advances in Electron and Light Optical imaging in biology and Medicine Ed. A. P. Somlyo. New York, The N.Y. Academy of Sciences.

Taylor, K. A., M.-H. Ho and A. Martonosi (1986). Image analysis of the Ca2+ -ATPase from sarcoplasmic reticulum. Annals of the New York Academy of Sciences: Recent Advances in Electron and Light Optical imaging in biology and Medicine Ed. A. P. Somlyo. New York, The N.Y. Academy of Sciences.

Gogol, E. P. and R. A. Capaldi (1990). Subunit arrangement of and rearrangements in E. coli F1F0 ATP synthase determined by cryo-electron microscopy. Proc. XII Int'l. Cong. Elec. Microsc. (Seattle) 1:240-241.

Gogol, E. P., E. Johnston, R. Aggeler and R. A. Capaldi (1990) Ligand-dependent structural variations in "Escherichia coli" F(1) ATPase revealed by cryoelectron microscopy. Proc. Nat. Acad. Sci. USA 87:9585-9589.

Lücken, U., E. P. Gogol and R. A. Capaldi (1990) Structure of the ATP synthase complex (ECF1F0) of Escherichi coli from cryoelectron microscopy. Biochem 29:5339-5343.

Misra, M., H. C. Beall, K. A. Taylor and H. P. Ting-Beall (1990) Configuration of subunits within crystals of Na, K- ATPase maintained in the frozen-hydrated state. J. Struct. Biol. 105:67-74.

Stokes, D. L. and N. M. Green (1990) Structure of CaATPase: electron microscopy of frozen- hydrated crystals at 6Å resolution in projection. J. Mol. Biol. 213:529-538.

Maunsbach, A. B., E. Zellmann and E. Skriver (1991) Cryo-electron microscope analysis of frozen-hydrated two- dimensional Na,K-ATPase crystals. Micron 22:57-58.

Aggeler, R., R. A. Capaldi, S. Dunn and E. P. Gogol (1992) Epitope mapping of monoclonal antibodies to the Escherichia coli F1 ATPase alpha subunit in relation to activity effects and location in the enzyme complex based on cryoelectron microscopy. Arch. Biochem. Biophys. 296:685-690.

Calcium Release Channel

Radermacher, M., T. Wagenknecht, R. Grassucci, J. Frank, M. Inui, C. Chadwick and S. Fleischer (1992) Cryo-EM of the native structure of the calcium release channel/ryanodine receptor from sarcoplasmic reticulum. Biophys J 61:936-940.

Cytochrome Oxidase

Valpuesta, J. M., R. Henderson and T. G. Frey (1990) Electron cryo-microscopic analysis of crystalline cytochrome oxidase. J. Mol. Biol. 214:237-251.

Gap Junction

Milligan, R. A., A. Brisson and P. N. T. Unwin (1984) Molecular structure determination of crystalline specimens in frozen aqueous solutions. Ultramicrosc. 13:1-10.

Unwin, P. N. T. and P. D. Ennis (1984) Two configurations of a channel-forming membrane protein. Nature 307:609-613.

Sosinsky, G. E., T. S. Baker, D. L. D. Caspar, Goodenough and D. A. (1990) Correlation analysis of gap junction lattice images. Biophys. J. 58:1213-1226.

Mitochondrial Outer Membrane

Guo, X.-W. (1990). Cryo-electron microscopy and correlation averaging of frozen- hydrated, polymorphic 2D crystals of the mitochondrial outer membrane channel. Proc. XII Int'l. Cong. Elec. Microsc. (Seattle) 1:100-101.

Guo, X. W., P. R. Smith, M. Radermacher and C. A. Mannella (1992) Structure of Crystalline VDAC, the Voltage-Gated Channel in the Mitochondrial Outer Membrane. Proc. Elect. Microsc. Soc. Am. 50:440-441.

Guo, X. W. and C. A. Mannella (1993) Conformational change in the mitochondrial channel, VDAC, detected by electron cryo-microscopy. Biophys. J. 64:545-549.

Nuclear Pore Complex

Akey, C. W. (1989) Interactions and structure of the nuclear pore complex revealed by cryo-electron microscopy. J. Cell Biol. 109:955-970.

Akey, C. W. and M. Radermacher (1993) Architecture of the Xenopus Nuclear Pore Complex revealed by Three- Dimensional Cryo-Electron Microscopy. J. Cell Biol. 122:1-19.

Porins

Chang, C.-F. and R. M. Glaeser (1983) Structural investigation of frozen-hydrated Omp C specimens prepared by the fatty acid monolayer technique. Elec. Microsc. Soc. Am. Proc. 41:734-735.

Purple Membrane

Hayward, S. B., D. A. Grano, R. M. Glaeser and K. A. Fisher (1978) Molecular orientation of bacteriorhodopsin within the purple membrane of halobacterium halobium. Proc. Natl. Acad. Sci. USA 75:4320-4324.

Hayward, S. B. and R. M. Glaeser (1980). Use of low temperatures for electron diffraction and imaging of biological macromolecular arrays. Electron Microscopy at Molecular Dimensions. (Eds., W.Baumeister & W. Vogell) Springer-Verlag, Berlin. pp. 226-233.

Hayward, S. B. and R. M. Stroud (1981) Projected structure of purple membrane determined to 3.7 angstroms resolution by low temperature electron microscopy. J. Mol. Biol. 151:491-517.

Studer, D., H. Gross, A. Stemmer and K.-H. Muller (1982) Cryo-electron microscopy of the purple membrane. Proc. Tenth Int'l. Cong. Elec. Microsc. (Hamburg) 2:455-456.

Studer, D., H. Gross, K.-H. Muller and A. Stemmer (1983) Electron microscopy of the orthorhombic purple membrane at 4.2 K. Ultramicrosc. 11:75-80.

Henderson, R., J. M. Baldwin, K. H. Downing, J. Lepault and F. Zemlin (1986) Structure of purple membrane from Halobacterium halobium: Recording, measurement and evaluation of electron micrographs at 3.5Å resolution. Ultramicrosc. 19:147-178.

Jaffe, J. S. and R. M. Glaeser (1987) Difference fourier analysis of surface features of bacteriorhodopsin using glucose-embedded and frozen-hydrated purple membrane. Ultramicrosc. 23:17-28.

Henderson, R., J. M. Baldwin, T. A. Ceska, F. Zemlin, E. Beckmann and K. H. Downing (1990) Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J Mol. Biol. 213:899-929.

Fujiyoshi, Y., K. Mitsuoka, T. Hirai, K. Murata, A. Miyazawa and Y. Kimura (1995) Characteristic feature on structure analyzed by high- resolution electron crystallography. JMSA Proceed. Microsc. Microanal. 53:834-835.

Other Membranes

Milligan, R. A., A. Brisson and P. N. T. Unwin (1984) Molecular structure determination of crystalline specimens in frozen aqueous solutions. Ultramicrosc. 13:1-10.

Lepault, J., F. Pattus and N. Martin (1985) Cryo-electron microscopy of artificial biological membranes. Biochim. Biophys. Acta 820:315-318.

Unwin, N. (1986). The use of cryoelectron microscopy in elucidating molecular design and mechanisms. Annals of the New York Academy of Sciences: Recent Advances in Electron and Light Optical imaging in biology and Medicine Ed. A. P. Somlyo. New York, The N.Y. Academy of Sciences.

Lücken, U. (1990). Electron-spectroscopic imaging (ESI) of frozen hydrated lipid vesicles and membrane proteins: A comparison with TEM. Proc. XII Int'l. Cong. Elec. Microsc. (Seattle) 1:508-509.

Nahoaki, K. P., Y. D. Akiko, Y. C. Akiyasu, S. B. Satoshi and F. Yoshinori (1990). High resolution cryo-electron microscopy sheds a new light upon biomembrane architecture. Proc. XII Int'l. Cong. Elec. Microsc. (Seattle) 1:494-495.

Schmid, M. F., B. R. DasGupta and J. P. Robinson (1990). Ordered arrays of Type B botulinum toxin on phospholipid vesicles. Proc. XII Int'l. Cong. Elec. Microsc. (Seattle) 1:496-497.

Walter, A., P. K. Vinson, A. Kaplun and Y. Talmon (1991) Intermediate structures in the cholate- phosphatidylcholine vesicle-micelle transition. Biophys J 60:1315-1325.

Kuhlbrandt, W. (1992) Two-dimensional crystallization of membrane proteins. Quart. Rev. Biophys. 25:1-49.

Lücken, U. and J. Jager (1992) The structure of membranes and membrane proteins embedded in amorphous ice. Proc. Elect. Microsc. Soc. Am. 50:432-433.


Microtubules

Mandelkow, E.-M. and E. Mandelkow (1985) Unstained microtubules studied by cryo-electron microscopy: Substructure, supertwist and disassembly\. J. Mol. Biol. 181:123-135.

Mandelkow, E. and E.-M. Mandelkow (1986). Quick-frozen microtubules studied by cryoelectron microscopy and image processing. Annals of the New York Academy of Sciences: Recent Advances in Electron and Light Optical imaging in biology and Medicine Ed. A. P. Somlyo. New York, The N.Y. Academy of Sciences.

Mandelkow, E.-V., R. Rapp and E. Mandelkow (1986) Microtubule structure studied by quick freezing: Cryo-electron microscopy and freeze fracture. J. Microsc. 141:361-373.

Mandelkow, E.-M., E. Mandelkow, M. and R. A. (1991) Microtubule dynamics and microtubule caps: a time-resolved cryo-electron microscopy study. J. Cell Biol. 114:977-991.

Chretien, D., F. Metoz, F. Verde, E. Karsenti and R. H. Wade (1992) Lattice defects in microtubules: Protofilament numbers vary within individual microtubules. J. Cell Biol. 117:1031-1040.

Wade, R. H. and D. Chretien (1993) Cryoelectron microscopy of microtubules. J. Struct. Biol. 110:1-27.

Meeting Abstracts, Newsletters and Bulletins

Chretien, D., D. Job and R. H. Wade (1990). Observations of frozen hydrated microtubules. Proc. XII Int'l. Cong. Elec. Microsc. (Seattle) 1:504-505.

Mandelkow, E.-M. and R. Milligan (1990). Time-resolved cryo-electron microscopy of oscillating microtubules. Proc. XII Int'l. Cong. Elec. Microsc. (Seattle) 1:502-503.


Muscle and Muscle-Related Structures

Trachtenberg, S., D. Stokes, E. Bullitt and D. DeRosier (1986) Actin and flagellar filaments: Two helical structures with variable twist. Annals of the New York Academy of Sciences: Recent Advances in Electron and Light Optical imaging in biology and Medicine 483:88-99.

Trinick, J., J. S. Cooper and E. H. Egelman (1986) Cryo-electron microscopy and three-dimensional reconstruction of actin filaments. J. Microsc. 141(3):349-360.

Milligan, R. A. and P. F. Flicker (1987) Structural relationships of actin, myosin, and tropomyosin revealed by cryo-electron microscopy. J. Cell Biol. 105:29-39.

Menetret, J.-F., W. Hofmann and J. Lepault (1988) Cryo-electron microscopy of insect flight muscle thick filaments. An approach to dynamic electron microscope studies. J. Mol. Biol. 202:175-178.

Cabral-Lilly, D., G. N. J. Phillips, G. E. Sosinsky, , L. Melanson, S. Chacko and C. Cohen (1991) Structural studies of tropomyosin by cryoelectron microscopy and x-ray diffraction. Biophys. J. 59:805-814.

Schmid, M. F., P. Matsudaira, T.-W. Jeng, J. Jakana, , E. Towns-Andrews, J. Bordas and W. Chiu (1991) Crystallographic analysis of acrosomal bundle from limulus sperm. J. Mol. Biol. 221:711-725.

Padron, R., M. Granados, L. Alamo, J. R. Guerrero and R. Craig (1992) Visualization of myosin helices in sections of rapidly frozen relaxed tarantula muscle. J. Struct. Biol. 108:269-276.

Schmid, M. F., J. Jakana, P. Matsudaira and W. Chiu (1992) Effects of radiation damage with 400-kV electrons on frozen, hydrated actin bundles. J. Struc. Biol. 108:62-68.

Schroder, R. R., W. Hofmann, J.-F. Menetret, K. C. Holmes and R. S. Goody (1992) Cryo-electron microscopy of vitrified muscle samples. Elect. Microsc. Rev. 5:171-192.

Vibert, P. (1992) Helical reconstruction of frozen-hydrated scallop myosin filaments. J. Mol. Biol. 223:661-671.

Avila-Sakar, A. J., M. F. Schmid, L.-S. Li, F. G. Whitby, G. N. P. Jr and W. Chiu (1993) Preliminary electron crystallographic analysis of ice-embedded tropomyosin crystals. J. Struct. Biol. 110:67-74.

Rayment, I., H. M. Holden, M. Whittaker, C. B. Yohn, M. Lorenz, K. C. Holmes and R. A. Milligan (1993) Structure of the actin-myosin complex and its implications for muscle contraction. Science 261:58-65.

Schmid, M. F., J. Jakana, P. Matsudaira and W. Chiu (1993) Imaging frozen, hydrated acrosomal bundle from limulus sperm at 7 angstroms resolution with a 400kV electron cryomicroscope. J. Mol. Biol. 230:384-386.

Lepault, J., J.-L. Ranck, I. Erik and M.-F. Carlier (1994) Small angle x-ray scattering and electron cryomicroscopy study of actin filaments: Role of the bound nucleotide in the structure of F-Actin. J. Struct. Biol. 112:79-91.

Meeting Abstracts, Newsletters, Bulletins

Lepault, J., H. Delacroix, I. Erk, G. Nicolas and J.-L. Ranck (1990). Cryo-electron microscopy of muscle and muscular components. Proc. XII Int'l. Cong. Elec. Microsc. (Seattle) 1:250-251.

Milligan, R. A., M. Whittaker and D. Safer (1990). Localization of cys374 of actin by cryo-EM and image analysis of undecagold-labeled filaments. Proc. XII Int'l. Cong. Elec. Microsc. (Seattle) 1:246-247.

Trinick, J. and H. White (1990). Cryo-electron microscopy of the acto-myosin-ATP complex. Proc. XII Int'l. Cong. Elec. Microsc. (Seattle) 1:248-249.

Jakana, J., M. F. Schmid, P. Matsudaria and W. Chiu (1992) High resolution spot scan imaging of frozen, hydrated actin bundles with 400kv electrons. Elec. Microsc. Soc. Am. Proc. 50:512-513.

Schmid, M. F., J. Jakana, P. Matsudaira and W. Chiu (1995) Comparison of 13 angstrom helical and 7Å crystallographic projection maps of frozen, hydrated acrosomal bundle from Limulus sperm. JMSA Proc. Microsc. Microanal. 53:850-851.


Other Macromolecules and Macromolecule Complexes

Schatz, M. and M. VanHeel (1990) Invariant classification of molecular views in electron micrographs. Ultramicrosc. 32:255-264.

Kedersha, N. L., J. E. Heuser, D. C. Chugani and L. H. Rome (1991) Vaults III. Vault ribonucleoprotein particles open into flower-like structures with octagonal symmetry. J. Cell Biol. 112:225-235.

Rao, S. P. S., M. D. Poojary, B. W. E. Jr, L. A. Melanson, B. Oriel and C. Cohen (1991) Fibrinogen structure in projection at 18Å resolution: Electron density by co-ordinated cryo-electron microscopy and x-ray crystallography. J Mol. Biol. 222:89-98.

Frank, J. and M. Radermacher (1992) Three-dimensional reconstruction of single particles negatively stained or in vitreous ice. Ultramicrosc. 46:241-262.

Kolatkar, P. R., M. A. Oliveira, M. G. Rossmann, A. H. Robbins, S. K. Katti, H. Hoover-Litty, C. Forte, J. M. Greve, A. McClelland and N. H. Olson (1992) Preliminary x-ray crystallographic analysis of intercellular adhesion molecule-1. J. Mol. Biol. 225:1127-1130.

Meeting Abstracts, Newsletters, Bulletins

Winkler, H., T. Schnyder and U. Lücken (1990). Electron microscopic comparison of frozen-hydrated with negatively stained and rotary-shadowed creatine kinase single molecules. Proc. XII Int'l. Cong. Elec. Microsc. (Seattle) 1:262-263.

Frank, J. (1991). New challenges to image processing posed by cryo-electron microscopy of single particles. Proc. Elect. Microsc. Soc. Am. 49:422-423.

Dube, P., H. Stark, E. V. orlova, M. Schatz, E. Beckmann, F. Zemlin and M. vanHeel (1995) 3D structure of single macromolecules at 15Å resolution by cryo-microscopy and angular reconstitution. JMSA Proc. Microsc. Microanal. 53:838-839.


Protein Crystals

Meeting Abstracts, Newsletters and Bulletins

Zemlin, F. and E. Beckmann (1990). High-resolution cryo-electron microscopy of 2-D protein crystals. Proc. XII Int'l. Cong. Elec. Microsc. (Seattle) 1:84-85.

Chiu, W., J. Brink, T. Soejima and M. Schmid (1992) Protein Electron Crystallography by 400KV Cryo-Microscopy. Proc. Elect. Microsc. Soc. Am. 50:1054-1055.

Burmester, C., K. C. Holmes and R. R. Schroder (1995) Multiple isomorphous replacement for phase determination in protein crystals. JMSA Proc. Microsc. Microanal. 53:856-857.


Respiratory Proteins

van Bruggen, E. F. J. (1986) Electron microscopy of hemocyanins 1942-1986. Micron Microsc. Acta 17:167-173.

Meeting Abstracts, Newsletters, Bulletins

Schatz, M., J. Jager and J. van Heel (1990). Molecular views of ice-embedded Lumbricus terrestris erythrocruorin obtained by invariant classification. Proc. XII Int'l. Cong. Elec. Microsc. (Seattle) 1:450-451.

Lewis, M. R. and R. Josephs (1992) Cryo-Electron Microscopy of Deoxy-Sickle Hemoglobin Fibers. Proc. Elect. Microsc. Soc. Am. 50:1036-1037.


Ribosomes

Milligan, R. A., A. Brisson and P. N. T. Unwin (1984) Molecular structure determination of crystalline specimens in frozen aqueous solutions. Ultramicrosc. 13:1-10.

Unwin, N. (1986). The use of cryoelectron microscopy in elucidating molecular design and mechanisms. Annals of the New York Academy of Sciences: Recent Advances in Electron and Light Optical imaging in biology and Medicine Ed. A. P. Somlyo. New York, The N.Y. Academy of Sciences.

Wagenknecht, T., R. Grassucci and J. Frank (1988) Electron microscopy and computer image averaging of ice-embedded large ribosomal subunits from Escherichia coli. J. Mol. Biol. 199:137-147.

Frank, J., P. Penczek, R. Grassucci and S. Srivastava (1991) Three-dimensional reconstruction of the 70S Escherichia coli ribosome in ice: the distribution of ribosomal RNA. J. Cell Biol. 115:597-605.

Frank, J. and M. Radermacher (1992) Three-dimensional reconstruction of single particles negatively stained or in vitreous ice. Ultramicroscopy 46:241-262.

Penczek, P., M. Radermacher and J. Frank (1992) Three-dimensional reconstruction of single particles embedded in ice. Ultramicrosc. 40:33-53.

Penczek, P. A., R. A. Grassucci and J. Frank (1994) The ribosome at improved resolution: new techniques for merging and orientation refinement in 3D cryo-electron microscopy of biological particles. Ultramicrosc. 53:251-270.

Frank, J., J. Zhu, P. Penczek, Y. Li, S. Srivastava, A. Verschoor, M. Radermacher, R. Grassucci, R. K. Lata and R. K. Agrawal (1995) A model of protein synthesis based on cryo-electron microscopy of the E. coli ribosome. Nature 376:441-444.

Meeting Abstracts, Newsletters, Bulletins

Milligan, R. A. and P. N. T. Unwin (1983) The native structure of the eukaryotic ribosome. Elec. Microsc. Soc. Am. Proc. 41:432-433.

Penczek, P., S. Srivastava and J. Frank (1990). The structure of the 70S E. coli ribosome in ice. Proc. XII Int'l. Cong. Elec. Microsc. (Seattle) 1:506-507.

Verschoor, A., R. Milligan, S. Srivastava and J. Frank (1990). Structural studies on the eukaryotic ribosome. Proc. XII Int'l. Cong. Elec. Microsc. (Seattle) 1:256-257.

Frank, J. (1991). New challenges to image processing posed by cryo- electron microscopy of single particles. Elec. Microsc. Soc. Am. Proc. 49:422-423 .

Frank, J. (1992) Density-Based Discrimination of Protein and RNA in the Ribosome. Proc. Elect. Microsc. Soc. Am. 50:464-465.

Milligan, R. A. and P. N. T. Unwin (1983) The native structure of the eukaryotic ribosome. Elec. Microsc. Soc. Am. Proc. 41:432-433.


Surface Layers/Cell Walls

Lepault, J. and T. Pitt (1984) Projected structure of unstained, frozen-hydrated T-layer of Bacillus brevis. EMBO J. 3:101-105.

Dickson, M. R., K. H. Downing, W. H. Wu and R. M. Glaeser (1986) Three-dimensional structure of the surface layer protein of aquaspirillum serpens vha determined by electron crystallography. J. Bact. 167:1025-1034.

Rachel, R., V. Jakabowski, H. Tietz, R. Hegerel and W. Baumeister (1986) Projected structure of the surface protein of Deinococcus radiodurans determined to 8Å resolution by cryomicroscopy. Ultramicrosc. 20:305-316.

Guckenberger, R., W. Wiegrabe, A. Hillebrand, T. Hartman, Z. Wang and W. Baumeister (1989) Scanning tunneling microscopy of a hydrated bacterial surface protein. Ultramicrosc. 31:327-332.

Wiegrabe, W., M. Nonnenmacher, R. Guckenberger and O. Wolter (1991) Atomic force microscopy of a hydrated bacterial surface protein. J. Microsc. 163:79-84.

Lembcke, G., W. Baumeister, E. Beckmann and F. Zemlin (1993) Cryo-electron microscopy of the surface protein of Sulfolobus shibatae. Ultramicrosc. 49:397-406.

Meeting Abstracts, Newsletters, Bulletins

Wu, W. H. and R. M. Glaeser (1983) Structural analysis of the surface-layer protein of spirillum serpens by high-resolution electron microscopy. Elec. Microsc. Soc. Am. Proc. 41:738-739.

Lembcke, G. and F. Zemlin (1990). Projected structure of the surface protein of Sulfolobus spec B12 determined to a resolution of 1.0 nm by cryo- electron microscopy. Proc. XII Int'l. Cong. Elec. Microsc. (Seattle) 1:102-103.



Toxic Proteins

Botulinum Neurotoxin

Flicker, P. F., V. S. Kulkarni, J. P. Robinson, G. Stubbs and B. R. DasGupta (1992) Cryo-electron microscopy of two-dimensional crystals of reduced type B botulinum neurotoxin. Proc. Elect. Microsc. Soc. Am. 50:530-531.

Schmid, M. F., J. P. Robinson and B. R. DasGupta (1993) Direct visualization of botulinum neurotoxin-induced channels in phospholipid vesicles. Nature 364:827-830.

Cholera Toxin

Mosser, G., V. Mallouh and A. Brisson (1992) A 9Å two-dimensional projected structure of cholera toxin B-subunit-Gm1 complexes determined by electron crystallography. J. Mol. Biol. 226:23-28.

Crotoxin

Jeng, T. W. and W. Chiu (1983) Electron crystallography of crotoxin complex thin crystals. Elec. Microsc. Soc. Am. Proc. 41:430-431.

Degn, L. L. (1987) Imaging of the crotoxin crystal in vitreous ice at 3.9Å resolution. Proc. Elect. Microsc. Soc. Am. 45:646-647.

Brink, J., W. Chiu and M. Dougherty (1992) Computer-controlled spot-scan imaging of crotoxin complex crystals with 400 keV electrons at near-atomic resolution. Ultramicrosc. 46:229-240.

Brink, J. and W. Chiu (1994) Applications of a slow-scan CCD camera in protein electron crystallography. J. Struc. Biol. 113:23-34.


Viruses

Reviews

Adrian, M., J. Dubochet, J. Lepault and A. W. McDowall (1984) Cryo-electron microscopy of viruses. Nature 308:32-36.

Horne, R. W. (1985). The development and application of electron microscopy to the structure of isolated plant viruses. Molecular Plant Virology. (Ed. J. W. Davies) CRC PressBoca Raton, Fl. pp. 1-41.

Dubochet, J. (1987) Cryo-electron microscopy of viruses in native state. Micron Microsc. Acta 18:333-334.

Booy, F. P. (1993). Cryoelectron microscopy. Viral Fusion Mechanisms Ed. J. Bentz. Boca Raton, CRC Press. pp. 21-51.

Helical

Lepault, J. (1985) Cryo-electron microscopy of helical particles TMV and T4 polyheads. J. Microsc. 140:73-80.

Lepault, J. and K. Leonard (1985) Three-dimensional structure of unstained, frozen-hydrated extended tails of bacteriophage T4. J. Mol. Biol. 182:431-441.

Jeng, T.-W., R. A. Crowther, G. Stubbs and W. Chui (1989) Visualization of a-helices in tobacco mosaic virus by cryo-electron microscopy. J. Mol. Biol. 205:251-257.

Henderson, R. (1992) Image contrast in high-resolution electron microscopy of biological macromolecules: TMV in ice. Ultramicrosc. 46:1-18.

Spherical

Vogel, R. H., S. W. Provencher, C.-H. Bonsdorff, M. Adrian, and J. Dubochet (1986) Envelope structure of semiliki forest virus reconstructed from cryo-electron micrographs. Nature 320:533-535.

Fuller, S. D. (1987) The T=4 envelope of sindbis virus is organized by interactions with a complementary T=3 capsid. Cell 48:923-934.

Fuller, S. D. and P. Argos (1987) Is sindbis a simple picornavirus with an envelope? EMBO J. 6:1099-1105.

Prasad, B. V. V., G. J. Wang, J. P. M. Clerx and W. Chiu (1987) Cryo electron microscopy of spherical viruses: An application to rotaviruses. Micron 18:327-331.

Baker, T. S., J. Drak and M. Bina (1988) Reconstruction of the three-dimensional structure of Simian virus 40 and visualization of the chromatin core. Proc. Natl. Acad. Sci. USA 85:422-426.

Newcomb, W. W., J. C. Brown, F. P. Booy and A. C. Steven (1989) Nucleocopsid mass and capsomer protein stoichiometry in equine herpesvirus 1: Scanning transmission electron microscopic study. J. Virol. 63:3777-3783.

Olson, N. H. and T. S. Baker (1989) Magnification calibration and the determination of spherical virus diameters using cryo-microscopy. Ultramicrosc. 30:281-298.

Schrag, J. D., B. V. V. Prasad, F. J. Rixon and W. Chiu (1989) Three-dimensional structure of the hsv1 nucleocapsid. Cell 56:651-660.

Baker, T. S., W. W. Newcomb, F. P. Booy, J. C. Brown, and A. C. Steven (1990) Three-dimensional structures of maturable and abortive capsids of equine herpesvirus 1 from cryoelectron microscopy. J. Virol. 64:563-573.

Prasad, B. V. V., G. J. Wang, J. P. M. Clerx and W. Chiu (1988) Three-dimensional structure of rotavirus. J. Mol. Biol. 199:269-275.

Provencher, S. W. and R. H. Vogel (1988) Three-dimensional reconstruction from electron micrographs of disordered specimens. I. Method. Ultramicrosc. 25:209-222.

Vogel, R. H. and S. W. Provencher (1988) Three-dimensional reconstruction from electron micrographs of disordered specimens. II. Implementation and results. Ultramicrosc. 25:223-240.

Yamaguchi, M., T. Hirano, H. Hirokawa, K. Sugahara, H. Mizokami and K. Matsubara (1988) Cryo-electron microscopy of Hepatitis B virus core particles produced by transformed yeast: Comparison with negative staining and ultrathin sectioning. J. Elec. Microsc. 36:337-341.

Baker, T. S., J. Drak and M. Bina (1989) The capsid of small papova viruses contains 72 pentameric capsomeres: Direct evidence from cryo-electron-microscopy of simian virus 40. Biophys. J. 55:243-253.

Olson, N. H., T. S. Baker, J. E. Johnson and D. A. Hendry (1990) The three-dimensional structure of frozen-hydrated Nudaurelia Capensis beta virus, a T=4 insect virus. J. Struc. Biol. 105:111-122.

Prasad, B. V. V., J. W. Burns, E. Marietta, M. K. Estes, and W. Chiu (1990) Localization of vp4 neutralization sites in rotavirus by three-dimensional cryo-electron microscopy. Nature 343:476-479.

Baker, T. S., W. W. Newcomb, N. H. Olson, L. M. Cowsert, , C. Olson and J. C. Brown (1991) Structures of bovine and human papillomaviruses: Analysis by cryoelectron microscopy and three-dimensional image reconstruction. Biophys. J. 60:1445-1456.

Booy, F. P., W. W. Newcomb, B. L. Trus, J. C. Brown, T. S. Baker, and A. C. Steven (1991) Liquid-crystalline, phage-like packing of encapsidated DNA in Herpes Simplex virus. Cell 64:1007-1015.

Yeager, M., K. A. Dryden, N. H. Olson, H. B. Greenberg, and T. S. Baker (1990) Three-dimensional structure of rhesus rotavirus by cryoelectron microscopy and image reconstruction. J. Cell Biol. 110:2133-2144.

Anthony, I. D., S. Bullivant, S. Dayal, A. R. Bellamy, and J. A. Berriman (1991) Rotavirus spike structure and polypeptide composition. J. Virol. 65:4334-4340.

Cyrklaff, M., I. Tews, S. D. Fuller and W. Kuhlbrandt (1991) High resolution of non-crystalline specimens: Cryo-electron microscopy of adenovirus. Micron 22:31-32.

Metcalf, P., M. Cyrklaff and M. Adrian (1991) The three-dimensional structure of reovirus obtained by cryo-electron microscopy. EMBO J. 10:3129-3136.

Montross, L., S. Watkins, R. B. Moreland, H. Mamon, D. L. D. Caspar and R. L. Garcea (1991) Nuclear assembly of polyomavirus capsids in insect cells expressing the major capsid protein VP1. J.Virol. 65:4991-4998.

Stewart, P. L., R. M. Burnett, M. Cyrklaff and S. D. Fuller (1991) Image reconstruction reveals the complex molecular organization of adenovirus. Cell 67:145-154.

Adrian, M., P. A. Timmins and J. Witz (1992) In vitro decapsidation of turnip yellow mosaic virus investigated by cryo-electron microscopy: a model for the decapsidation of a small isometric virus. J Gen. Virol. 73:2079-2083.

Cheng, R. H., N. H. Olson and T. S. Baker (1992) Cauliflower mosaic virus: A 420 subunit (T=7), multilayer structure. Virology 186:655-668.

Dokland, T., B. H. Lindqvist and S. D. Fuller (1992) Image reconstruction from cryo-electron micrographs reveals the morphopoietic mechanism in the p2-p4 bacteriophage system. EMBO J. 839 -846.

Hewat, E. A., T. F. Booth, P. T. Loudon and P. Roy (1992) Three-dimensional reconstruction of baculovirus expressed bluetongue virus core-like particles by cryo-electron microscopy. Virology 189:10-20.

Hewat, E. A., T. F. Booth, R. W. Wade and P. Roy (1992) 3-D reconstruction of bluetongue virus tubules using cryoelectron microscopy. J. Struct. Biol. 108:35-48.

Hewatt, E. A., T. F. Booth and P. Roy (1992) Structure of bluetongue virus particles by cryoelectron microscopy. J. Struct. Biol. 109:61-69.

Kenney, J. M., J. Hantula, S. D. Fuller, L. Mindich, P. M. Ojala and D. H. Bamford (1992) Bacteriophage f6 envelope elucidated by chemical cross-linking, immunodetection, and cryoelectron microscopy. Virology 190:635-644.

McKenna, R., D. Xia, P. Willingmann, L. L. Ilag, , S. Krishnaswamy, M. G. Rossmann, N. H. Olson, T. S. Baker and N. L. Incardona (1992) Atomic structure of single-stranded DNA bacteriophage fx174 and its functional implications. Nature 355:137-143.

Olson, N. H., T. S. Baker, P. Willingmann and N. L. Incardona (1992) The three-dimensional structure of frozen-hydrated bacteriophage fx174. J. Struc. Biol. 108:168-175.

Prasad, B. V., S. Yamaguchi and P. Roy (1992) Three-dimensional structure of single-shelled bluetongue virus. J. Virol. 66:2135-2142.

Stubbs, G. (1992) Atomic structure of single-stranded DNA bacteriophage FX 174 and its functional implications. Chemtracts-Biochem. Mol. Biol. 3:136-139.

Trus, B. L., W. W. Newcomb, F. P. Booy, J. C. Brown, and A. C. Steven (1992) Distinct monoclonal antibodies separately label the hexons or the pentons of herpes simplex virus capsid. Proc. Natl. Acad. Sci. USA 89:11508-11512.

Wang, G.-J., C. Porta, Z. Chen, T. S. Baker and J. E. Johnson (1992) Identification of a Fab interaction footprint site on an icosahedral virus by cryoelectron microscopy and x-ray crystallography. Nature 355:275-278.

Conway, J. F., B. L. Trus, F. P. Booy, W. W. Newcomb, J. C. Brown and A. C. Steven (1993) The effects of radiation damage on the structure of frozen hydrated HSV-1 capsids. J. Struc. Biol. 111:222-233.

Dokland, T., M. L. Isaksen, S. D. Fuller and B. H. Lindqvist (1993) Capsid localization of the bacteriophage P4 psu protein. Virology 194:682-687.

Dryden, K. A., G. Wang, M. Yeager, M. L. Nibert, K. M. Coombs, , D. B. Furlong, B. N. Fields and T. S. Baker (1993) Early steps in reovirus infection are assoiciated with dramatic changes in supramolecular structure and protein conformation: Analysis of virions and subviral particles by cryoelectron microscopy and image reconstruction. J. Cell Biol. 122:1023-1041.

Harrison, S. C. (1993) Common cold virus. Proc. Nat. Acad. Sci. USA 90:783.

Hogle, J. M. (1993) The viral canyon. Current Biology 3:278-281.

Newcomb, W. W., B. L. Trus, F. P. Booy, A. C. Steven, J. Wall, S. and J. C. Brown (1993) Structure of the Herpes Simplex virus capsid. Molecular composition of the pentons and the triplexes. J. Mol. Biol. 232:499-511.

Olson, N. H., P. R. Kolatkar, M. A. Oliveira, R. H. Cheng, , J. M. Greve, A. McClelland, T. S. Baker and M. G. Rossmann (1993) Structure of a human rhinovirus complexed with its receptor molecule. Proc. Natl. Acad. Sci. USA 90:507-511.

Paredes, A. M., D. T. Brown, R. Rothnagel, W. Chiu, Schoepp, R. J., R. E. Johnston and B. V. V. Prasad (1993) Three-dimensional structure of a membrane-containing virus. Proc. Natl. Acad. Sci. USA 90:9095-9099.

Prasad, B. V. V., P. E. Prevelidge, E. Marietta, R. O. Chen, , D. Thomas, J. King and W. Chiu (1993) Three-dimensional transformation of capsids associated with genome packaging in a bacterial virus. J. Mol. Biol. 231:65-74.

Rossmann, M. G., T. J. Smith and R. R. Rueckert (1993) The structure of human rhinovirus 14. Structure 0:xxiv-xxv.

Shaw, A. L., R. Rothnagel, D. Chen, R. F. Ramig, W. Chiu, and B. V. V. Prasad (1993) Three-dimensional visualization of the rotavirus hemagglutinin structure. Cell 74:693-701.

Smith, T. J., N. H. Olson, R. H. Cheng, E. S. Chase, Baker and T. S. (1993) Structure of a human rhinovirus-bivalently bound antibody complex: Implications for viral neutralization and antibody flexibility. Proc. Natl. Acad. Sci. USA 90:7015-7018.

Smith, T. J., N. H. Olson, R. H. Cheng, H. Liu, E. S. Chase, , W. M. Lee, D. M. Leippe, A. Mosser, R. G., R. R. , Baker and T. S. (1993) Structure of human rhinovirus complexed with Fab fragments from a neutralizing antibody. J. Virol. 67:1148-1158.

Stewart, P. L., S. D. Fuller and R. M. Burnett (1993) Difference imaging of adenovirus: bridging the resolution gap between x-ray crystallography and electron microscopy. EMBO J. 12:2589-259.

Thomas, J. M. (1993) Architecture of the invisible. Nature 364:478-482.

Cheng, R. H., J. R. Caston, G.-J. Wang, F. Gu, T. J. Smith, T. S. Baker, R. F. Bozarth, B. L. Trus, N. Cheng, R. B. Wickner and A. C. Steven (1994) Fungal virus capsids, cytoplasmic compartments for the replication of double-stranded RNA, formed as icosahedral shells of asymmetric Gag dimers. J. Mol. Biol. 244:255-258.

Cheng, R. H., V. S. Reddy, N. H. Olson, A. J. Fisher, T. S. Baker and J. E. Johnson (1994) Functional implications of quasi-equivalence in a T=3 icosahedral animal virus established in cryo-electron microscopy and x-ray crystallography. Structure 2:271-282.

Chiu, W. and T. J. Smith (1994) Structural studies of virus-antibody complexes by electron cryomicroscopy and X-ray crystallography. Curr. Opin. Struc. Biol. 4:219-224.

Crowther, R. A., N. A. Kiselev, B. Bottcher, J. A. Berriman, G. P. Borisova, V. Ose and P. Pumpens (1994) Three-dimensional structure of hepatitis B virus core particles determined by electron cryomicroscopy. Cell 77:943-950.

Hewat, E. A., T. F. Booth and P. Roy (1994) Structure of correctly self-assembled bluetongue virus- like particles. J. Struct. Biol. 112:183-191.

Liu, H., T. J. Smith, W.-M. Lee, A. G. Mosser, R. R. Rueckert, N. H. Olson, R. H. Cheng and T. S. Baker (1994) Structure determination of an Fab fragment that neutralizes human rhinovirus 14 and analysis of the Fab- virus complex. J. Mol. Biol. 240:127-137.

Porta, C., G. Wang, H. Cheng, Z. Chen, T. S. Baker and J. E. Johnson (1994) Direct imaging of interactions between an icosahedral virus and conjugate Fab fragments by cryoelectron microscopy and x-ray crystallography. Virology 204:777-788.

Rossmann, M. G., N. H. Olson, P. R. Kolatkar, M. A. Oliveira, R. H. Cheng, J. M. Greve, A. McClelland and T. S. Baker (1994) Crystallographic and cryo EM analysis of virion-receptor interactions. Arch. Virol. 9:531-541.

Stewart, P. L. (1994) Integrating cryo-electron microscopy into drug-design strategies. Trends Biotech. 12:429-431.

Stewart, P. L. and R. M. Burnett (1994) Spherical virus assembly. Curr Opin Struc Biol 4:213-218.

Venien-Bryan, C. and S. D. Fuller (1994) The organization of the spike complex of Semliki Forest virus. J. Mol. Biol. 236:572-583.

Wikoff, W. R., G. Wang, C. R. Parrish, R. H. Cheng, M. L. Strassheim, T. S. Baker and M. G. Rossmann (1994) The structure of a neutralized virus: canine parvovirus complexed with neutralizing antibody fragment. Structure 2:595-607.

Yeager, M., J. A. Berriman, T. S. Baker and A. R. Bellamy (1994) Three-dimensional structure of the rotavirus haemagglutinin VP4 by cryo-electron microscopy and difference map analysis. EMBO J. 13:1011-1018.

Zhou, Z. H., B. V. V. Prasad, J. Jakana, F. J. Rixon and W. Chiu (1994) Protein subunit structures in the herpes simplex virus A-capsid determined from 400kV spot-scan electron cryomicroscopy. J. Mol. Biol. 242:456-469.

Butcher, S. J., D. H. Bamford and S. D. Fuller (1995) DNA packaging orders the membrane of bacteriophage PRD1. EMBO J. 14:6078-6086.

Cheng, R. H., R. J. Kuhn, N. H. Olson, M. G. Rossmann, H.-K. Choi, T. J. Smith and T. S. Baker (1995) Nucleocapsid and glycoprotein organization in an enveloped virus. Cell 80:621-630.

Conway, J. F., R. L. Duda, N. Cheng, R. W. Hendrix and A. C. Steven (1995) Proteolytic and conformational control of virus capsid maturation: The bacteriophage HK97 system. J. Mol. Biol. 253:86-99.

Ilag, L. L., N. H. Olson, T. Dokland, C. L. Music, R. H. Cheng, Z. Bowen, R. McKenna, M. G. Rossmann, T. S. Baker and N. L. Incardona (1995) DNA packaging intermediates of bacteriophage FX174. Structure 3:353-363.

Kenney, J. M., C.-H. v. Bonsdorff, M. Nassal and S. D. Fuller (1995) Evolutionary conservation in the hepatitis B virus core structure: comparison of human and duck cores. Structure 3:1009-1019.

Smith, T. J., R. H. Cheng, N. H. Olson, P. Peterson, E. Chase, R. J. Kuhn and T. S. Baker (1995) Putative receptor binding sites on alphaviruses as visualized by cryoelectron microscopy. Proc. Natl. Acad. Sci. USA 92:10648-10652.

Smith, T. J., A. G. Mosser and T. S. Baker (1995) Structural studies on the mechanisms of antibody-mediated neutralization of human rhinovirus. Sem. Virol. 6:233-242.

Speir, J. A., S. Munshi, G. Wang, T. S. Baker and J. E. Johnson (1995) Structures of the native and swollen forms of cowpea chlorotic mottle virus determined by x-ray crystallography and cryo-electron microscopy. Structure 3:63-78.

Zhao, X., J. M. Fox, N. H. Olson, T. S. Baker and M. J. Young (1995) In Vitro assembly of cowpea chlorotic mottle virus from coat protein expressed in Escherichia coli and in Vitro-trascribed viral cDNA. Virology 207:486-494.

Belnap, D. M., N. H. Olson, N. M. Cladel, W. W. Newcomb, J. C. Brown, J. W. Kreider, N. D. Christensen and T. S. Baker (1996) Conserved features in papillomavirus and polyomavirus capsids. J. Mol. Biol. 259:249-263.

Chipman, P. R., M. Agbandje-McKenna, S. Kajigaya, K. E. Brown, N. S. Young, T. S. Baker and M. G. Rossmann (1996) Cryo-electron microscopy studies of empy capsids of human parvovirus B19 complexed with its cellular receptor. Proc. Natl. Acad. Sci. USA 93:7502-7506.

Conway, J. F., B. L. Trus, F. P. Booy, W. W. Newcomb, J. C. Brown and A. C. Steven (1996) Visualization of three-dimensional density maps reconstructed from cryoelectron micrographs of viral capsids. J. Struct. Biol. 116:200-208.

Fuller, S. D., S. J. Butcher, R. H. Cheng and T. S. Baker (1996) Three-dimensional reconstruction of icosahedral particles -- The uncommon line. J. Struct. Biol. 116:48-55.

Prasad, B. V. V., R. Rothnagel, C. Q.-Y. Zeng, J. Jakana, J. A. Lawton, W. Chiu and M. K. Estes (1996) Visualization of ordered genomic RNA and localization of transcriptional complexes in rotavirus. Nature 382:471-473.

Non-symmetric

Booy, F. P., R. W. H. Ruigrok and E. F. J. VanBruggen (1985) Electron microscopy of Influenza virus. A comparison of negatively stained and ice-embedded particles. J. Mol. Biol. 184:667-676.

Talmon, Y., C. Prasad B. V. V., W. J. P. M., C. G-J., W., H. and M. J. (1987) Electron microscopy of vitrified-hydrated La Crosse virus. J. Virol. 61:2319-2321.

Baschong, W., U. Aebi, C. Baschong-Prescianotto, J. Dubochet, L. Landmann, E. Kellenberger and M. Wurtz (1988) Head structure of bacteriophages T2 and T4. J. Ultrastructure and Molecular Structure Research 99:189-202.

Guo, P., S. Erickson, W. Xu, N. H. Olson, T. S. Baker and D. Anderson (1991) Regulation of the Phage F 29 prohead shape and size by the portal vertex. Virology 183:366-373.

Ruigrok, R. W. H. and E. A. Hewat (1991) Comparison of negatively stained and frozen hydrated samples of influenza viruses A and B and of vesicular stomatitis virus. Micron 22:423-434.

Wang, G.-J., M. Hewlett and W. Chiu (1991) Structural variation of La Crosse virions under different chemical and physical conditions. Virology 184:455-459.

Fujiyoshi, Y., N. P. Kume, K. Sakata and S. B. Sato (1994) Fine structure of influenza A virus observed by electron cryo-microscopy. EMBO J. 13:318-326.

Meeting Abstracts, Newsletters and Bulletins

Baker, T. S., J. Drak and M. Bina (1985) Cryo-electron microscopy and image analysis of SV40. Elec. Microsc. Soc. Am. Proc. 43:316-317.

Olson, N. H., T. S. Baker, W. Bomu, J. E. Johnson, Hendry and D. A. (1987) The three-dimensional structure of frozen-hydrated Nudaurelia Capensis beta virus. Elec. Microsc. Soc. Am. Proc. 45:650-651.

Booy, F. B., W. W. Newcomb, J. C. Brown and A. C. Steven (1988) Herpesvirus nucleocapsids imaged in the frozen-hydrated state. Elec. Microsc. Soc. Am. Proc. 46:164-165.

Frederik, P. M., K. N. J. Burger, M. C. A. Stuart and A. J. Verkleij (1990). Lipid polymorphism and virus-membrane fusion as observed in vitrified thin films by cryo-electron microscopy. Proc. XII Int'l. Cong. Elec. Microsc. (Seattle) 1:492-493.

Baker, T. S., W. W. Newcomb, F. P. Booy, J. C. Brown, and A. C. Steven (1989) Three-dimensional reconstructions of 'light' and 'intermediate' capsids of equine herpes virus. Elec. Microsc. Soc. Am. Proc. 47:822-823.

Baker, T. S., N. H. Olson, W. W. Newcomb, J. C. Brown, and C. Olson (1989) Electron microscopy of stained and unstained bovine papilloma virus: Comparison with polyoma virus. Elec. Microsc. Soc. Am. Proc. 47:820-821.

Cheng, R. H., N. H. Olson and T. S. Baker (1989) Cryo-electron microscopy of cauliflower mosaic virus. Elec. Microsc. Soc. Am. Proc. 47:824-825.

Langmore, J. P., M. F. Smith and D. A. Rankert (1990). Quantitative energy-filtered cryo-EM of hydrated chromosome fibers, viruses, and heavy atoms. Proc. XII Int'l. Cong. Elec. Microsc. (Seattle) 1:252-253.

Olson, N. H., W. Xu, W. D. Grochulski, D. L. Anderson, Baker and T. S. (1990) Electron microscopy of negatively stained and frozen hydrated bactriophage f29. Proc. XII Int'l. Cong. Elec. Microsc. (Seattle) 1:270-271.

Prasad, B. V. V., E. Marietta, J. W. Burns, M. K. Estes and W. Chiu (1990). Three-dimensional structure of rotavirus-FAB complex. Proc. XII Int'l. Cong. Elec. Microsc. (Seattle) 1:238-239.

Wang, G., K. A. Dryden, K. M. Coombs, D. B. Furlong, Baker and T. S. (1990) Cryo-electron microscopy of reovirus intermediate subviral 1 particles. Proc. Twelfth Int'l. Cong. Elec. Microsc. (Seattle) 1:276-277.

Baker, T. S. (1992) Cryo-electron microscopy and three-dimensional image reconstruction of icosahedral viruses. Electron Microsc. EUREM 92, Granada, Spain 3:275-279.

Baker, T. S., R. H. Cheng, J. E. Johnson, N. H. Olson, G. J. Wang and T. J. Schmidt (1992) Organized Packing of RNA Inside Viruses as Revealed by Cryo-Electron Microscopy and X-Ray Diffraction Analysis. Proc. Elect. Microsc. Soc. Am. 50:454-455.

Booy, F. P., B. L. Trus, W. W. Newcomb, J. C. Brown, P. Serwer and A. C. Steven (1992) Organization of dsDNA in Icosahedral Virus Capsids. Proc. Elect. Microsc. Soc. Am. 50:452-453.

Charest, P. M., J. Jakana, M. F. Schmid, S. Vidal, D. Kolakofsky and W. Chiu (1992) Electron cryo-microscopy of nucleocapsids of sendai virus. Proc. Elect. Microsc. Soc. Am. 50:870-871.

Conway, J. F., B. L. Trus, F. P. Booy, W. W. Newcomb, J. C. Brown and A. C. Steven (1992) Effects of Radiation Damage on Frozen Hydrated Capsids of HSV-1. Proc. Elect. Microsc. Soc. Am. 50:532-533.

Misra, M., B. L. Trus, P. Wingfield and A. C. Steven (1992) Helical Polymers of the REV Protein of Human Immunodeficiency Virus 1. Proc. Elect. Microsc. Soc. Am. 50:456-457.

Olson, N. H., T. J. Smith, P. R. Kolatkar, M. A. Oliveira, R. R. Rueckert, J. M. Greve, M. G. Rossman and T. S. Baker (1992) Cryoelectron Microscopy of Complexes of Human Rhinovirus with a Monoclonal Fab and the Viral Cellular Receptor. Proc. Elect. Microsc. Soc. Am. 50:524-525.

Steven, A. C., W. W. Newcomb, F. P. Booy, J. C. Brown and B. L. Trus (1992) Immuno-Electron Microscopy at Sub-Nanometer Resolution. Proc. Elect. Microsc. Soc. Am. 50:522-523.

Wang, G.-J., C. Porta, Z. Chen, R. H. Cheng, T. S. Baker and J. E. Johnson (1992). The analysis of a spherical virus-fab interaction by cryo-electron microscopy and x-ray crystallography. Electron Microscopy II, 5th Asia-Pacific Electron Microscopy Conference Eds. K. H. Kuo and Z. H. Zhai. River Edge, NJ, World Scientific Publishing Co.

Baker, T. S., R. H. Cheng, V. S. Reddy, N. H. Olson, A. J. Fisher and J. E. Johnson (1994) Cryo-electron microscopy and x-ray crystallographic studies of Flock House virus, a T=3 icosahedral animal virus (invited). ICEM Paris 13:525-526.

Grimm, R. and W. Baumeister (1995) Low-dose energy-filtered TEM of frozen hydrated virus particles using a post-column energy filter. JMSA Proc. Microsc. Microanal. 53:844-845.

Stewart, P. L. and G. R. Nemerow (1995) Combining structures from cryo-electron microscopy and x- ray crystallography. JMSA Proc. Microsc. Microanal. 53:44-45.

Zhou, Z. H., J. He, J. Jakana, J. D. Tatman, F. J. Rixon and W. Chiu (1995) Assembly of VP26 in Herpes simplex virus-1 capsid implicated by 3d structure of recombinant capsid. JMSA Proc. Microsc. Microanal. 53:840-841.

Ziese, U., D. typke, R. Hegerl and W. Baumeister (1995) Cryo electron microscopy of SSV1 phage particles. JMSA Proc. Microsc. Microanal. 53:842-843.

Booy, F. B., H. L. Greenstone, R. B. S. Roden, J. T. Shiller, A. C. Steven and B. L. Trus (1996). High resolution studies of papillomavirus and herpes simplex virus. EUREM, Dublin, Ireland,

Trus, B. L., H. L. Greenstone, R. B. S. Roden, J. T. Schiller and F. P. Booy (1996). 3D reconstruction of bovine papilloma virus visualized at 9Å. Int'l Biophysics Congress, Amsterdam,

Crystallization Methods

Ward, R. J., J.-F. Menetret, F. Pattus and K. Leonard (1990) Method for forming two-dimensional paracrystals of biological filaments on lipid monolayers. J. Elect. Microsc. Tech. 14:335-341.

Kuhlbrandt, W. (1992) Two-dimensional crystallization of membrane proteins. Quart. Rev. Biophys. 25:1-49.

Schnyder, T., M. Cyrklaff, K. Fuchs and T. Wallimann (1994) Crystallization of mitochondrial creatine kinase on negatively charged lipid layers. J. Struct. Biol. 112:136-147.


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Last edited April 29, 1997