Molecular mechanism for the crystallization of bacteriorhodopsin in lipidic cubic phases

FEBS Letters

Nollert, Peter³  Qiu, Hong¹  Rosenbusch, Jurg P²  Caffrey, Martin¹  Landau, Ehud M² 

[1] Biochemistry, Biophysics, Chemistry, Ohio State University, 100 W. 18th Avenue, Columbus, OH 43210, USA;Biozentrum, University of Basel, Klingelbergstr. 70, CH-4056 Basel, Switzerland;Department of Biochemistry and Biophysics, University of California San Francisco, 513 Parnassus, San Francisco, CA 94134-0448, USA

关键词: Crystallization;    Bacteriorhodopsin;    Lipidic cubic phases;    bR;    bacteriorhodopsin;    MO;    monoolein;    OG;    β-octyl glucopyranoside;   

DOI  :  10.1016/S0014-5793(01)02747-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Crystals of transmembrane proteins may be grown from detergent solutions or in a matrix of membranous lipid bilayers existing in a liquid crystalline state and forming a cubic phase (in cubo). While crystallization in micellar solutions appears analogous to that for soluble proteins, crystallization in lipidic matrices is poorly understood. As this method was shown to be applicable to several membrane proteins, understanding its mechanism will facilitate a rational design of crystallization, minimizing the laborious screening of a large number of parameters. Using polarization microscopy and low-angle X-ray diffraction, experimental evidence is provided to support a mechanistic model for the in cubo crystallization of bacteriorhodopsin in a lipid matrix. Membrane proteins are thought to reside in curved lipid bilayers, to diffuse into patches of lower curvature and to incorporate into lattices which associate to form highly ordered three-dimensional crystals. Critical testing of this model is necessary to generalize it to other membrane proteins.

【 授权许可】

Unknown