title: Expression, purification, crystallization and preliminary crystallographic analysis of recombinant pteridine reductase of Trypanosoma cruzi.
abstract: The recombinant version of Trypanosoma cruzi pteridine reductase was expressed in Escherichia coli, purified to homogeneity from the soluble fraction of bacterial extract by metal-chelate affinity chromatography and crystallized in the presence of the cofactor (NADPH) and an inhibitor (methotrexate) at 295 K using sodium acetate as precipitant. The crystals are trigonal, belonging to space group P3(1) (or P3(2)), with unit-cell parameters a = 74.35, c = 179.96 A under cryogenic conditions. The asymmetric unit contains a tetramer, with a corresponding V(M) of 2.3 A(3) Da(-1)and a solvent content of 46%. Native data have been collected to 2.1 A resolution using Cu Kalpha X-rays.
authors.affiliation: Division of Geographic Medicine, School of Medicine and Center for Biophysical Sciences and Engineering, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
authors.forename: N
authors.initials: N
authors.lastname: Schormann
authors.forename: B
authors.initials: B
authors.lastname: Pal
authors.forename: D
authors.initials: D
authors.lastname: Chattopadhyay
mesh_terms: D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli; D009249:NADP / Q000737:chemistry; D010088:Oxidoreductases / Q000096:biosynthesis / Q000737:chemistry*; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry; D014349:Trypanosoma cruzi / Q000201:enzymology*
chemical_list: D011994:Recombinant Proteins; D009249:NADP; D010088:Oxidoreductases; C085592:pteridine reductase