1kme
From Proteopedia
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CRYSTAL STRUCTURE OF BACTERIORHODOPSIN CRYSTALLIZED FROM BICELLES
Overview
Obtaining crystals of membrane proteins that diffract to high resolution, remains a major stumbling block in structure determination. Here we, present a new 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, A, b=108.9 A, c=55.9 A, beta=113.58 degrees and a dimeric asymmetric unit., The structure was solved by molecular replacement and refined at 2.0 A, 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.
About this Structure
1KME is a Single protein structure of sequence from Halobacterium salinarum with GLC, RET and SQU as ligands. Full crystallographic information is available from OCA.
Reference
Bicelle crystallization: a new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure., Faham S, Bowie JU, J Mol Biol. 2002 Feb 8;316(1):1-6. PMID:11829498
Page seeded by OCA on Tue Nov 20 19:21:58 2007
Categories: Halobacterium salinarum | Single protein | Bowie, J.U. | Faham, S. | GLC | RET | SQU | Membrane protein
