Three-dimensional crystallization of membrane proteins
- 1 November 1988
- journal article
- review article
- Published by Cambridge University Press (CUP) in Quarterly Reviews of Biophysics
- Vol. 21 (4), 429-477
- https://doi.org/10.1017/s0033583500004625
Abstract
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 ofRhodopseudomonas viridis(Deisenhoferet al.1984, 1985) and ofRhodobacter sphaeroides(Allenet al.1986, 1987a, 6; Changet 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.Keywords
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