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Crystallization in cubo:: general applicability to membrane proteins

被引：85
作者：
Chiu, ML
Nollert, P
Loewen, MC
Belrhali, H
Pebay-Peyroula, E
Rosenbusch, JP
Landau, EM
机构：
[1] Univ Basel, Bioctr, Dept Mol Microbiol, CH-4056 Basel, Switzerland
[2] European Synchrotron Radiat Facil, F-38043 Grenoble, France
[3] Univ Grenoble 1, F-38027 Grenoble, France
[4] CNRS, CEA, Inst Biol Struct, F-38027 Grenoble 1, France
来源：
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2000年 / 56卷
关键词：
D O I：
10.1107/S0907444900004716
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
Obtaining well ordered crystals of membrane proteins is the single most serious stumbling block in the pursuit of their high-resolution structures. The applicability of lipidic cubic phase-mediated crystallization is demonstrated on a diverse set of bacterial membrane proteins: two photosynthetic reaction centres, a light-harvesting complex and two retinal proteins, halorhodopsin and bacteriorhodopsin. Despite marked differences in molecular dimensions, subunit composition and membrane origin, one single lipid, monoolein, is sufficient to form a crystallization matrix for all the aforementioned systems. Therefore, the lipidic cubic phase approach is proposed as a general method for crystallizing membrane proteins.
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收藏
页码：781 / 784
页数：4
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