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_2006_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_62_136
Author(s) : Biswal BK , Garen G , Cherney MM , Garen C , James MN
Ref : Acta Crystallographica Sect F Struct Biol Cryst Commun , 62 :136 , 2006
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.

PubMedSearch : Biswal_2006_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_62_136
PubMedID: 16511284
Gene_locus related to this paper: myctu-ephB

Related information

Inhibitor Diphenylurea
Gene_locus myctu-ephB
Family Epoxide_hydrolase
Structure 2E3J    2ZJF

Citations formats

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 Commun 62 :136

Biswal BK, Garen G, Cherney MM, Garen C, James MN (2006)
Acta Crystallographica Sect F Struct Biol Cryst Commun 62 :136