Paper Report for: Biswal_2006_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_62_136
Reference
Title: Cloning, expression, purification, crystallization and preliminary X-ray studies of epoxide hydrolases A and B from Mycobacterium tuberculosis Biswal BK, Garen G, Cherney MM, Garen C, James MN Ref: Acta Crystallographica Sect F Struct Biol Cryst Commun, 62:136, 2006 : PubMed
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.
Biswal BK, Garen G, Cherney MM, Garen C, James MN (2006) Cloning, expression, purification, crystallization and preliminary X-ray studies of epoxide hydrolases A and B from Mycobacterium tuberculosis Acta Crystallographica Sect F Struct Biol Cryst Commun62: 136-8
Biswal BK, Garen G, Cherney MM, Garen C, James MN (2006) Acta Crystallographica Sect F Struct Biol Cryst Commun62: 136-8