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CRYSTALLIZATION OF MONODISPERSE MALTOPORIN FROM WILDTYPE AND MUTANT STRAINS OF VARIOUS ENTEROBACTERIACEAE

被引：15
作者：
KELLER, TA
FERENCI, T
PRILIPOV, A
ROSENBUSCH, JP
机构：
[1] UNIV BASEL,BIOZENTRUM,DEPT MICROBIOL,CH-4056 BASEL,SWITZERLAND
[2] UNIV SYDNEY,DEPT MICROBIOL G08,SYDNEY,NSW 2006,AUSTRALIA
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1994年 / 199卷 / 02期
关键词：
D O I：
10.1006/bbrc.1994.1295
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：
Maltoporin has been purified by affinity chromatography on starch gel columns. This single-step procedure affords the rapid purification of active protein from wild-type and mutants of E. coli, and from other Gram-negative bacteria. The monodisperse protein was crystallized under various conditions. Several preparations have yielded crystals amendable to X-ray analysis, notably a single cysteine substitution, S57C. (C) 1994 Academic Press, Inc. Maltoporin
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页码：767 / 771
页数：5
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