Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 316, Issue 1, Pages 1-6Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1006/jmbi.2001.5295
Keywords
membrane protein; crystals; crystallization; lipid cubic phase; detergent
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Funding
- NIGMS NIH HHS [R01 GM59164, R01 GM63919] Funding Source: Medline
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Obtaining crystals of membrane proteins that diffract to high resolution remains a major stumbling block in structure determination. Here we present a now method for crystallizing membrane proteins from a bicelle forming lipid/detergent mixture. The method is flexible and simple to use. As a test case, bacteriorhodopsin (bR) from Halobacterium salinarum was crystallized from a bicellar solution, yielding a new bR crystal form. The crystals belong to space group P2(1) with unit cell dimensions of a = 45.0 Angstrom, b = 108.9 Angstrom, c = 55.9 Angstrom, beta = 113.58degrees and a dimeric asymmetric unit. The structure was solved by molecular replacement and refined at 2.0 Angstrom resolution. In all previous bR structures the protein is organized as a parallel trimer, but in the crystals grown from bicelles, the individual bR subunits are arranged in an antiparallel fashion. (C) 2002 Elsevier Science Ltd.
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