Crystallization of membrane proteins

Current Opinion in Structural Biology

Volumn 7, Issue 5, 1997, Pages 697-701

  Ostermeier, Christian ^a   Michel, Hartmut ^b  

^a YALE UNIVERSITY   (United States)

^b MAX PLANCK INSTITUTE OF BIOPHYSICS   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CYTOCHROME C OXIDASE; DETERGENT; MEMBRANE PROTEIN; MITOCHONDRIAL ENZYME; UBIQUINOL CYTOCHROME C REDUCTASE;

COMPLEX FORMATION; CRYSTAL STRUCTURE; CRYSTALLIZATION; MICELLE; NONHUMAN; PHOTOTROPHIC BACTERIUM; PRIORITY JOURNAL; PROTEIN STRUCTURE; SHORT SURVEY; TECHNIQUE; X RAY CRYSTALLOGRAPHY;

EID: 0030785122     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(97)80080-2     Document Type: Article

References (25)

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25. Landau EM, Rosenbusch JP. Lipidic cubic phases: a novel concept for the crystallization of membrane proteins. Proc Natl Acad Sci USA. 93:1996;14532-14535 Bacteriorhodopsin is crystallized using a system consisting of lipids, which form bicontinuous cubic bilayer phases, salts, water, and protein. Bacteriorhodopsin prepared in octylglucoside is incorporated into the lipids. The lipidic phase should act as a sink for the detergent molecules so that the bacteriorhodopsin molecules diffuse in the membrane system of the lipids without their detergent micelle. The lipid phases are suggested to provide nucleation sites and support crystal growth by lateral diffusion of the protein molecules in the bilayer membrane. of outstanding interest.