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Lipidic Cubic Phases: A Novel Concept for the Crystallization of Membrane Proteins
Ehud M. Landau and Jurg P. Rosenbusch
Proceedings of the National Academy of Sciences of the United States of America
Vol. 93, No. 25 (Dec. 10, 1996), pp. 14532-14535
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/41118
Page Count: 4
You can always find the topics here!Topics: Crystals, Cubic crystals, Membrane proteins, Lipids, Crystallization, Hexagonal crystals, Detergents, Wave diffraction, Crystallography, Crystal growth
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Understanding the mechanisms of action of membrane proteins requires the elucidation of their structures to high resolution. The critical step in accomplishing this by x-ray crystallography is the routine availability of well-ordered three-dimensional crystals. We have devised a novel, rational approach to meet this goal using quasisolid lipidic cubic phases. This membrane system, consisting of lipid, water, and protein in appropriate proportions, forms a structured, transparent, and complex three-dimensional lipidic array, which is pervaded by an intercommunicating aqueous channel system. Such matrices provide nucleation sites (``seeding'') and support growth by lateral diffusion of protein molecules in the membrane (``feeding''). Bacteriorhodopsin crystals were obtained from bicontinuous cubic phases, but not from micellar systems, implying a critical role of the continuity of the diffusion space (the bilayer) on crystal growth. Hexagonal bacteriorhodopsin crystals diffracted to 3.7 angstrom resolution, with a space group P63, and unit cell dimensions of a = b = 62 angstrom, c = 108 angstrom; α = β = 90 degrees and γ = 120 degrees.
Proceedings of the National Academy of Sciences of the United States of America © 1996 National Academy of Sciences