Macromolecular structure determination by electron microscopy: new advances and recent results

Macromolecular structure determination by electron microscopy: new advances and recent results Electron microscopy is undergoing a mini-renaissance, as a number of biological systems are yielding to higher resolution analysis as a result of advances in instrumentation, specimen preparation and image-processing technology. The atomic structure of tubulin has now been solved, crucial elements of secondary structure have recently been revealed in several membrane proteins (rhodopsin, gap junctions, aquaporin, and Ca 2+ and H + ATPases) and in a virus particle, and macromolecular complexes are being seen in increasingly fine detail. This growth has been enhanced further by the ability to combine structures of macromolecular complexes derived by electron microscopy with X-ray structures of their components, in order to reconstruct molecular machines and large multiprotein complexes in immense detail. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Current Opinion in Structural Biology Elsevier

Macromolecular structure determination by electron microscopy: new advances and recent results

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Publisher
Elsevier
Copyright
Copyright © 1998 Elsevier Ltd
ISSN
0959-440x
DOI
10.1016/S0959-440X(98)80150-4
Publisher site
See Article on Publisher Site

Abstract

Electron microscopy is undergoing a mini-renaissance, as a number of biological systems are yielding to higher resolution analysis as a result of advances in instrumentation, specimen preparation and image-processing technology. The atomic structure of tubulin has now been solved, crucial elements of secondary structure have recently been revealed in several membrane proteins (rhodopsin, gap junctions, aquaporin, and Ca 2+ and H + ATPases) and in a virus particle, and macromolecular complexes are being seen in increasingly fine detail. This growth has been enhanced further by the ability to combine structures of macromolecular complexes derived by electron microscopy with X-ray structures of their components, in order to reconstruct molecular machines and large multiprotein complexes in immense detail.

Journal

Current Opinion in Structural BiologyElsevier

Published: Oct 1, 1998

References

  • Electron-crystallographic refinement of the structure of bacteriorhodopsin
    Grigorieff, N; Ceska, TA; Downing, KH; Baldwin, JM; Henderson, R
  • Two-dimensional crystals of proteins on lipid layers
    Kornberg, RD; Darst, SA
  • Structural study of the response regulator HupR from Rhodobacter capsulatus . Electron microscopy of two-dimensional crystals on a nickel-chelating lipid
    Vénien-Bryan, C; Balavoine, F; Toussaint, B; Mioskowski, C; Hewat, EA; Helme, B; Vignais, PM
  • Functionalized lipid tubules as tools for helical crystallization of proteins
    Ringler, P; Muller, W; Ringsdorf, H; Brisson, A

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