Cloning, expression, purification, crystallization and preliminary X-ray studies of epoxide hydrolases A and B from Mycobacterium tuberculosis
- CIHR Group in Protein Structure and Function, Department of Biochemistry, University of Alberta, Edmonton T6G 2H7 (Canada)
Epoxide hydrolases A (Rv3617) and B (Rv1938), detoxification enzymes from M. tuberculosis, have been cloned, expressed, purified and crystallized. Crystals of Rv3617 and Rv1938 diffracted to 3.0 and 2.1 Å resolution, respectively. Mycobacterium tuberculosis epoxide hydrolases A and B, corresponding to open reading frames Rv3617 and Rv1938, are detoxification enzymes against epoxides. The recombinant forms of these enzymes have been expressed in Escherichia coli and purified to homogeneity. Diffraction-quality crystals of Rv3617 and Rv1938 were obtained by the hanging-drop vapour-diffusion technique. Crystals of Rv3617 and Rv1938 diffracted to 3.0 and 2.1 Å resolution, respectively, at the ALS synchrotron at Berkeley, CA, USA.
- OSTI ID:
- 22356261
- Journal Information:
- Acta Crystallographica. Section F, Vol. 62, Issue Pt 2; Other Information: PMCID: PMC2150947; PMID: 16511284; PUBLISHER-ID: en5149; OAI: oai:pubmedcentral.nih.gov:2150947; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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