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Three-dimensional crystallization of membrane proteins

Published online by Cambridge University Press:  17 March 2009

W. Kühlbrandt
W. Kühlbrandt
Affiliation:
Biophysics Section, Department of Physics, Imperial College, London SW7 2BZ, England
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Extract

As recently as 10 years ago, the prospect of solving the structure of any membrane protein by X-ray crystallography seemed remote. Since then, the threedimensional (3-D) structures of two membrane protein complexes, the bacterial photosynthetic reaction centres of Rhodopseudomonas viridis (Deisenhofer et al. 1984, 1985) and of Rhodobacter sphaeroides (Allen et al. 1986, 1987 a, 6; Chang et al. 1986) have been determined at high resolution. This astonishing progress would not have been possible without the pioneering work of Michel and Garavito who first succeeded in growing 3-D crystals of the membrane proteins bacteriorhodopsin (Michel & Oesterhelt, 1980) and matrix porin (Garavito & Rosenbusch, 1980). X-ray crystallography is still the only routine method for determining the 3-D structures of biological macromolecules at high resolution and well-ordered 3-D crystals of sufficient size are the essential prerequisite.

Type
Research Article
Information
Quarterly Reviews of Biophysics , Volume 21 , Issue 4 , November 1988 , pp. 429 - 477
Copyright
Copyright © Cambridge University Press 1988

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