1kme

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(New page: 200px<br /><applet load="1kme" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kme, resolution 2.00&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 17:14, 20 November 2007

Image:1kme.gif

1kme, resolution 2.00Å

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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

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