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Updated: Aug 11, 2026
Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins
Published on: June 20, 2019
Cloning, expression, purification, crystallization and preliminary X-ray studies of epoxide hydrolases A and B from
Bichitra K Biswal1, Grace Garen, Maia M Cherney
1CIHR Group in Protein Structure and Function, Department of Biochemistry, University of Alberta, Edmonton T6G 2H7, Canada.
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 A resolution, respectively, at the ALS synchrotron at Berkeley, CA, USA.
