Cloning, expression, purification, crystallization and preliminary X‐ray studies of epoxide hydrolases A and B from Mycobacterium tuberculosis

Publisher: John Wiley & Sons Inc

E-ISSN: 1744-3091|62|2|136-138

ISSN: 1744-3091

Source: Acta Crystallographica Section F, Vol.62, Iss.2, 2006-02, pp. : 136-138

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Abstract

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.