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

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: http://dx.doi.org/10.2174/0929866013409111

Publication date: 2001-12-01

• Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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• In this Subject: Anatomy & Physiology
• By this author: 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.

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