Preliminary X-Ray Crystallographic Studies Of The Mycobacterium Tuberculosis Hsp16.3 Molecular Chaperone

Authors: Chen Y.; An J.; Ding Y.; Dai H.; Mao Q.; Feng L.; Liu B.; Chang Y.; Chen F.; He H.; Tang H.; Chang Z.; Rao Z.

Source: Protein and Peptide Letters, Volume 8, Number 6, December 2001 , pp. 499-502(4)

Publisher: Bentham Science Publishers

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Abstract:

Mycobacterium Tuberculosis HSP16.3 is a major antigen maximally expressed during the stationary phase. Previous studies showed that HSP16.3 can function as a molecular chaperone in vitro. Here, crystallization trails of HSP 16.3 were reported. A kind of crystal can be diffracted to 2.8 A resolution at the ”Photon Factory“, a synchrotron light source in Japan. The crystal displayed the space group R3 with unit cell parameters a=b=110 A , c=152 A and gamma=120 degree. Assuming the presence of 9 HSP16.3 molecules in an asymmetric unit, it gives a Vm= 0.73 A 3 / Da. and solvent content of 35percent by volume.

Keywords: MYCOBACTERIUM TUBERCULOSIS HSP16.3; IPTG isopropyl ?-D-thiogalacto-pyranoside; MPD 2-Methyl-2,4-Pentanediol; sHSP small heat shock protein; MAD Multiwavelength Anomalous Dispersion; molecular chaperone activity

Language: English

Document Type: Review article

DOI: 10.2174/0929866013409111

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