Membranes


Index

  • Acetylcholine Receptor

  • ATPases

  • Calcuium Release Channel

  • Cytochrome Oxidase

  • Gap Junction

  • Mitochondrial Outer Menbrane

  • Nuclear Pore Complex

  • Porins

  • Purple Membrane

  • Other 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 Ca -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.



    Top of page

    Back to Vitrified Specimen Menu
    Last edited April 29, 1997