Abstract
The technical capabilities of electron diffraction and high resolution electron microscopy have recently been advanced to the point that three-dimensional density maps can be obtained at sufficiently high resolution to allow an interpretation in terms of the structure at atomic resolution. The high scattering intensity of electrons compared to x-rays results in the fact that two-dimensional crystals, one molecule thick, are ideal specimens for electron crystallography. In the event that large, well ordered, three-dimensional crystals cannot be obtained, which are required for x-ray diffraction, electron diffraction now represents a practical alternative for high resolution structure analysis. The conditions needed to obtain two-dimensional crystals are, in general, very different from those which can produce three-dimensional crystals. As a result, attempts to obtain two-dimensional crystals complement the more traditional approach, which would be to obtain crystals for x-ray crystallography.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Amos, L. A., Henderson, R. and Unwin, P. N. T. (1982) “Three-dimensional structure determination by electron microscopy of two-dimensional crystals”, Prog. Biophys. Mol. Biol. 39, 183–231.
Baldwin, J.M. and Henderson, R. (1984) “Measurement and evaluation of electrondiffraction patterns from two-dimensional crystals”, Ultramicroscopy 14, 319–336.
DeRosier, D. J. and Klug, A. (1968) “Reconstruction of three-dimensional structures from electron micrographs”, Nature 217, 130–134.
Downing, K. H. (1991) “Spot-scan imaging in transmission electron microscopy”, Science 251, 53–59.
Downing, K. H. and Chiu, W. (1990) “Cold stage design for high resolution electron microscopy of biological materials”, Electron Microsc. Rev. 3, 213–226.
Dubochet, J., Adrian, M., Chang, J. J., Homo, J.-C., Lepault, J., McDowall, A. W. and Shultz, P. (1988) “Cryo-electron microscopy of vitrified biological specimens”, Quart. Rev. Biophysics 21, 129–228.
Fromherz, P., Rocker, C. and Ruppel, D. (1986) “From discoid micelles to spherical vesicles. The concept of edge activity”, Faraday Discuss. Chem. Soc. 81, 39–48.
Fuller, S. D., Capaldi, R. A. and Henderson, R (1979) “Structure of cytochrome c oxidase in deoxycholate-derived two-dimensional crystals”, J. Mol. Biol. 134, 305–327.
Glaeser, R. M. (1982) “Electron microscopy”, in G. Ehrenstein and H. Lecar (eds.) Methods of Experimental Physics: Biophysics, Vol 20, Academic Press, New York, pp 391–444.
Glaeser, R. M. (1985) “Electron crystallography of biological macromolecules”, Ann. Rev. Phys. Chem. 36, 243–275.
Glaeser, R. M. and Ceska, T. A. (1989) “High-voltage electron diffraction from bacteriorhodopsin (purple membrane) is measurably dynamical”, Acta Cryst. A45, 620–628.
Glaeser, R. M., Zilker, A., Radermacher, M., Gaub, H. E., Hartmann, T. and Baumeister, W. (1991) “Interfacial energies and surface-tension forces involved in the preparation of thin, flat crystals of biological macromolecules for high-resolution electron microscopy”, J. Microscopy 161, 21–45.
Hayward, S. B. and Glaeser, R. M. (1979) “Radiation damage of purple membrane at low temperature”, Ultramicroscopy 4, 201–210.
Henderson, R. and Glaeser, R. M. (1985) “Quantitative analysis of image contrast in electron micrographs of beam-sensitive crystals”, Ultramicroscopy 16, 139–150.
Henderson R., Baldwin, J. M., Ceska, T. A., Zemlin, F., Beckmann, E. and Downing, K. H., (1990) “Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy”, J. Mol. Biol. 213, 899–929.
Henderson, R. and Unwin, P. N. T. (1975) “Three-dimensional model of purple membrane obtained by electron microscopy”, Nature 257, 28–32.
Ho, M. H., Jap, B. K. and Glaeser, R. M. (1988) “Validity domain of the weak-phase-object approximation for electron diffraction of thin protein crystals”, Acta Cryst. A44, 878–884.
Hoppe, W., Langer, R., Knesch, G. and Poppe, Ch. (1968) “Protein-Kritallstruktur analyse mit Elektronenstrahlen”, Naturwissenschaften 55, 333–336.
Jap, B. K. (1988) “High-resolution electron diffraction of reconstituted PhoE porin”, J. Mol. Biol. 205, 407–419.
Jap, B. K., Walian, P. J. and Gehring, K. (1991) “Structural architecture of an outer membrane channel as determined by electron crystallography”, Nature 350, 167–170.
Kong, T. (1989) “Reconstitution of halorhodopsin”, PhD Thesis, University of California, Berkeley.
Kuhlbrandt, W. (1987) “Three-dimensional crystals of the light-harvesting chlorophylla/b protein complex from pea chloroplasts”, J. Mol. Biol. 194, 757–762.
Kuhlbrandt, W. (1992) “Two-dimensional crystallization of membrane proteins”, Quart.Rev. Biophys. In Press.
Kuhlbrandt, W. and Wang, D. N. (1991) “Three-dimensional structure of plant light-harvesting complex determined by electron crystallography”, Nature 350, 130–134.
Leonard, K., Haiker, H. and Weiss, H. (1987) “Three-dimensional structure of NADH:ubiquinone reductase (complex I) fromNeurosporamitochondria determined by electron microscopy of membrane crystals”, J. Mol. Biol. 194, 277–286.
Mannella, C. A. (1984) “Phospholipase-induced crystallization of channels in mitochondrial outer membranes”, Science 224, 165–166.
Mohraz, M., Simpson, M. V. and Smith, P. R. (1987) “The three-dimensional structure of the Na,K-ATPase from electron microscopy”, J. Cell Biol. 105, 1–8.
Sass, H. J., Buldt, G., Beckmann, E., Zemlin, F., van Heel, M., Zeitler, E., Rosenbusch, J. P., Dorset, D. L. and Massalski, A. (1989) “Densely packed ß-structure at the protein-lipid interface of porin is revealed by high-resolution cryo-electron microscopy”, J. Mol. Biol. 209, 171–175.
Sikerwar, S. S., Downing, K. H. and Glaeser, R. M. (1991) “Three-dimensional structure of an invertebrate intracellular communicating junction”, J. Struct. Biol. 106, 255–263.
Steven, A. C., ten Heggeler, B., Muller, R., Kistler, J. and Rosenbusch, J. P. (1977) “Ultrastructure of a periodic protein layer in the outer membrane ofEschericia coli”J. Cell Biol. 72, 292–301.
Skriver, E., Maunsbach, A. B. and Jorgensen, P. L. (1981) “Formation of two-dimensional crystals in pure membrane-bound Na+K+-ATPase“, FEBS Lett. 131, 219–222.
Steven, A. C., ten Heggeler, B., Muller, R., Kistler, J. and Rosenbusch, J. P. (1977) “Ultrastructure of a periodic protein layer in the outer membrane ofEschericia coli”J. Cell Biol. 72, 292–301.
Stokes, D. L. and Green, N. M. (1990) “Three-dimensional crystals of CaATPase from sarcoplasmic reticulum”, Biophys. J. 57, 1–14.
Taylor, K., Dux, L. and Martonosi, A. (1984) “Structure of the vanadate-inducedcrystals of sarcoplasmic reticulum Ca2+-ATPase”, J. Mol. Biol. 174, 193–204.
Taylor, K. A. and Glaeser, R. M. (1974) “Electron diffraction of frozen, hydrated protein crystals”, Science 186, 1036–1037.
Toyoshima, C. and Unwin, N. (1990) “Three-dimensional structure of the acetylcholine receptor by cryoelectron microscopy and helical image reconstruction”, J. Cell Biol. 111, 2623–2635.
Unwin P. N. T. and Henderson, R. (1975) “Molecular structure determination by electron microscopy of unstained crystalline specimens”, J. Mol. Biol. 94, 425–440.
Unwin, P. N. T. and Ennis, P. D. (1984) “Two configurations of a channel-forming membrane protein” Nature 307, 609–613.
Unwin, N., Toyoshima, C. and Kubalek, E. (1988) “Arrangement of the acetylcholine receptor subunits in the resting and desensitized states, determined by cryoelectron microscopy of crystallizedTorpedopostsynaptic membranes” Nature 107, 1123–1138.
Walian, P. J. and Jap, B. K. (1990) “Three-dimensional electron diffraction of PhoE 0porin to 2.8A resolution”, J. Mol. Biol. 215, 429–438.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1992 Springer Science+Business Media Dordrecht
About this paper
Cite this paper
Glaeser, R.M. (1992). Electron Crystallography of Membrane Proteins. In: Pullman, A., Jortner, J., Pullman, B. (eds) Membrane Proteins: Structures, Interactions and Models. The Jerusalem Symposia on Quantum Chemistry and Biochemistry, vol 25. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-2718-9_1
Download citation
DOI: https://doi.org/10.1007/978-94-011-2718-9_1
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-010-5205-4
Online ISBN: 978-94-011-2718-9
eBook Packages: Springer Book Archive