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Protein & Peptide Letters


ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

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

Author(s): Y. Chen, J. An, Y. Ding, H. Dai, Q. Mao, L. Feng, B. Liu, Y. Chang, F. Chen, H. He, H. Tang, Z. Chang and Z. Rao

Volume 8, Issue 6, 2001

Page: [499 - 502] Pages: 4

DOI: 10.2174/0929866013409111

Price: $65


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 ß-D-thiogalacto-pyranoside, MPD 2-Methyl-2,4-Pentanediol, sHSP small heat shock protein, MAD Multiwavelength Anomalous Dispersion, molecular chaperone activity

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