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Mapping Lipid and Detergent Molecules at the Surface of Membrane Proteins

DOI: 10.1042/BST0390775 DOI Help
PMID: 21599648 PMID Help

Authors: Richard Cogdell (University of Glasgow)
Co-authored by industrial partner: No

Type: Conference Paper
Conference: Biochemical society Annual symposium
Peer Reviewed: Yes

State: Published (Approved)
Published: June 2011
Diamond Proposal Number(s): 1229

Abstract: Electron-density maps for the crystal structures of membrane proteins often show features suggesting binding of lipids and/or detergent molecules on the hydrophobic surface, but usually it is difficult to identify the bound molecules. In our studies, heavy-atom-labelled phospholipids and detergents have been used to unequivocally identify these binding sites at the surfaces of test membrane proteins, the reaction centres from Rhodobacter sphaeroides and Blastochloris viridis. The generality of this method is discussed in the present article.

Subject Areas: Biology and Bio-materials


Instruments: I02-Macromolecular Crystallography , I03-Macromolecular Crystallography , I04-Macromolecular Crystallography

Other Facilities: ESRF

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