Isolation, purification and preliminary X-ray characterization of Cpn60-2 (65 kDa heat-shock protein) from Mycobacterium tuberculosis.
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.
Adir
Noam
N
Department of Chemistry and Institute of Catalysis, Science and Technology, Technion, Israel Institute of Technology, Technion City, Haifa 32000, Israel. nadir@technion.ac.il
Dobrovetsky
Elena
E
Shafat
Itay
I
Cohen
Cyril
C
Kashi
Yechezkel
Y
D018834:Chaperonin 60 / Q000737:chemistry / Q000302:isolation & purification*; D002853:Chromatography, Liquid; D018360:Crystallography, X-Ray; D009169:Mycobacterium tuberculosis / Q000737:chemistry*; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification
D018834:Chaperonin 60; D011994:Recombinant Proteins