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

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

doi:10.1107/s0907444902010909

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

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

Technion-Israel Institute of Technology

Research output: Contribution to journal › Article › peer-review

2 Scopus citations

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 Å, β = 95.5°, and contain a dimer in the asymmetric unit. The crystals diffract to 4.0 Å using a Cu rotating-anode X-ray generator.

Original language	English
Pages (from-to)	1474-1475
Number of pages	2
Journal	Acta Crystallographica Section D: Biological Crystallography
Volume	58
Issue number	9
DOIs	https://doi.org/10.1107/s0907444902010909
State	Published - Sep 2002
Externally published	Yes

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

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 {\AA}, β = 95.5°, and contain a dimer in the asymmetric unit. The crystals diffract to 4.0 {\AA} using a Cu rotating-anode X-ray generator.",

author = "Noam Adir and Elena Dobrovetsky and Itay Shafat and Cyril Cohen and Yechezkel Kashi",

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T1 - Isolation, purification and preliminary X-ray characterization of Cpn60-2 (65 kDa heat-shock protein) from Mycobacterium tuberculosis

AU - Adir, Noam

AU - Dobrovetsky, Elena

AU - Shafat, Itay

AU - Cohen, Cyril

AU - Kashi, Yechezkel

PY - 2002/9

Y1 - 2002/9

N2 - 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 Å, β = 95.5°, and contain a dimer in the asymmetric unit. The crystals diffract to 4.0 Å using a Cu rotating-anode X-ray generator.

AB - 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 Å, β = 95.5°, and contain a dimer in the asymmetric unit. The crystals diffract to 4.0 Å using a Cu rotating-anode X-ray generator.

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

Abstract

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