1KME

CRYSTAL STRUCTURE OF BACTERIORHODOPSIN CRYSTALLIZED FROM BICELLES

Summary for 1KME

• Entry DOI: 10.2210/pdb1kme/pdb
• Descriptor: Bacteriorhodopsin, RETINAL, 2,10,23-TRIMETHYL-TETRACOSANE, ... (5 entities in total)
• Functional Keywords: membrane protein
• Biological source: Halobacterium salinarum
• Cellular location: Cell membrane; Multi-pass membrane protein: P02945
• Total number of polymer chains: 2
• Total formula weight: 52294.48

Authors

Faham, S.,Bowie, J.U. (deposition date: 2001-12-14, release date: 2002-02-13, Last modification date: 2024-11-20)

Primary citation

Faham, S.,Bowie, J.U.
Bicelle crystallization: a new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure.
J.Mol.Biol., 316:1-6, 2002

PubMed Abstract: 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.

PubMed: 11829498
DOI: 10.1006/jmbi.2001.5295

Experimental method

X-RAY DIFFRACTION (2 Å)