Crystallization of membrane proteins

被引:180
作者
Ostermeier, C [1 ]
Michel, H [1 ]
机构
[1] MAX PLANCK INST BIOPHYS,ABT MOL MEMBRANBIOL,D-60528 FRANKFURT,GERMANY
关键词
D O I
10.1016/S0959-440X(97)80080-2
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Five new membrane protein structures have been determined since 1995 using X-ray crystallography: bacterial light-harvesting complex; bacterial and mitochondrial cytochrome c oxidases; mitochondrial bc(1) complex; and a-hemolysin. These successes are partly based on advances in the crystallization procedures for integral membrane proteins. Variation of the size of the detergent micelle and/or increasing the size of the polar surface of the membrane protein is the most important route to well-ordered membrane protein crystals. The use of bicontinuous lipidic cubic phases also appears to be promising. (C) Current Biology Ltd ISSN 0959-440X
引用
收藏
页码:697 / 701
页数:5
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