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结核分枝杆菌中Cpn60-2(65 kDa热休克蛋白)的分离、纯化及初步X射线表征

Isolation, purification and preliminary X-ray characterization of Cpn60-2 (65 kDa heat-shock protein) from Mycobacterium tuberculosis.

作者信息

Adir Noam, Dobrovetsky Elena, Shafat Itay, Cohen Cyril, Kashi Yechezkel

机构信息

Department of Chemistry and Institute of Catalysis, Science and Technology, Technion, Israel Institute of Technology, Technion City, Haifa 32000, Israel.

出版信息

Acta Crystallogr D Biol Crystallogr. 2002 Sep;58(Pt 9):1474-5. doi: 10.1107/S0907444902010909. Epub 2002 Aug 23.

Abstract

Cpn60-2 is a member of a unique family of putative molecular chaperones homologous to GroEL (Cpn60) but of unknown function and found only in Mycobacterium tuberculosis and closely related species. Cpn60-2 has mainly been studied for its strong immunogenity. Here, the purification, crystallization and preliminary crystallographic analysis of M. tuberculosis Cpn60-2 are reported. The crystals belong to space group P2, with unit-cell parameters a = 57, b = 115.5, c = 81.5 A, beta = 95.5 degrees, and contain a dimer in the asymmetric unit. The crystals diffract to 4.0 A using a Cu rotating-anode X-ray generator.

摘要

Cpn60-2是一个独特的假定分子伴侣家族的成员,与GroEL(Cpn60)同源,但功能未知,仅在结核分枝杆菌及密切相关物种中发现。Cpn60-2主要因其强大的免疫原性而受到研究。在此,报道了结核分枝杆菌Cpn60-2的纯化、结晶及初步晶体学分析。晶体属于空间群P2,晶胞参数a = 57,b = 115.5,c = 81.5 Å,β = 95.5°,不对称单元中包含一个二聚体。使用铜旋转阳极X射线发生器,晶体衍射至4.0 Å。

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