Open AccessCloning, expression, purification, crystallization and preliminary X‐ray studies of epoxide hydrolases A and B from Mycobacterium tuberculosis
Author(s) -
Biswal Bichitra K.,
Garen Grace,
Cherney Maia M.,
Garen Craig,
James Michael N. G.
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106000637
Subject(s) - mycobacterium tuberculosis , escherichia coli , crystallization , enzyme , recombinant dna , epoxide , chemistry , tuberculosis , microbiology and biotechnology , biochemistry , biology , organic chemistry , catalysis , medicine , pathology , gene
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.