MEMBRANE-PROTEIN CRYSTALLIZATION - OBSERVATIONS AND USE OF SHORT CHAIN PHOSPHOLIPIDS AS AMPHIPHILES

被引：2

作者：

EISELE, JL

KELLER, TA

KONIG, N

STAUFFER, KA

ROSENBUSCH, JP

LOW, PS

机构：

[1] UNIV BASEL,BIOZENTRUM,MIKROBIOL ABT,CH-4056 BASEL,SWITZERLAND

[2] PURDUE UNIV,DEPT CHEM,W LAFAYETTE,IN 47907

来源：

JOURNAL OF CRYSTAL GROWTH | 1991年 / 110卷 / 1-2期

关键词：

D O I：

10.1016/0022-0248(91)90871-2

中图分类号：

O7 [晶体学];

学科分类号：

0702 ; 070205 ; 0703 ; 080501 ;

摘要：

An integral membrane protein, porin OmpF located in E. coli outer membrane, has been crystallized in the sole presence of short chain phospholipids. Although the amphiphilic characteristics of these molecules are comparable to those of conventional detergents, they appear to be unique probes for the study of the phospholipid-protein interactions by crystallographic methods. Here we also discuss the influence of the detergent head group on the crystal packing, and the role of additives. The stabilization of crystals after termination of growth in protein-free buffer is described.

引用

页码：96 / 102

页数：7

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