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

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

Author information

1
Department of Chemistry and Institute of Catalysis, Science and Technology, Technion, Israel Institute of Technology, Technion City, Haifa 32000, Israel. nadir@technion.ac.il

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.

PMID:
12198306
DOI:
10.1107/S0907444902010909
[Indexed for MEDLINE]

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