期刊
PROTEIN SCIENCE
卷 14, 期 1, 页码 148-158出版社
WILEY
DOI: 10.1110/ps.041022305
关键词
membrane protein; membrane protein expression; cloning; structural genomics; Mycobacterium tuberculosis; Escherichia coli
资金
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [P01GM064676] Funding Source: NIH RePORTER
- NIGMS NIH HHS [P01 GM64676, P01 GM064676] Funding Source: Medline
Seventy integral membrane proteins from the Mycobacterium tuberculosis genome have been cloned and expressed in Escherichia coli. A combination of T7 promoter-based vectors with hexa-His affinity tags and BL21 E. coli strains with additional IRNA genes to supplement sparsely used E. coli codons have been most successful. The expressed proteins have a wide range of molecular weights and number of transmembrane helices. Expression of these proteins has been observed in the membrane and insoluble fraction of E. coli cell lysates and, in some cases, in the soluble fraction. The highest expression levels in the membrane fraction were restricted to a narrow range of molecular weights and relatively few transmembrane helices. In contrast, overexpression in insoluble aggregates was distributed over a broad range of molecular weights and number of transmembrane helices.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据