title: Crystallization and preliminary crystallographic analysis of trypanothione reductase from Trypanosoma cruzi, the causative agent of Chagas' disease.
abstract: Trypanothione reductase from Trypanosoma cruzi is the most promising target molecule for the rational design of a specific drug against Chagas' disease. The recombinant protein was purified in a single chromatographic step and crystallized. Two crystal forms suitable for X-ray diffraction analysis were obtained. Tetragonal crystals (a = b = 87.4 A, c = 152.3 A) were grown from 30% polyethylene glycol (average M(r) = 8,000) in the presence of 0.2% beta-n-octylglucoside (space group either P4(2) with one dimer or P4(2)22 with one monomer in the asymmetric unit). Monoclinic crystals (space group P2, a = 136.3 A, b = 91.1 A, c = 126.0 A, beta = 94 degrees) were grown from 1.2 M sodium citrate in the presence of 2% octanoyl-N-methyl-glucamide. They contain two dimers of the enzyme in the asymmetric unit; both crystal forms diffract to 3 A resolution.
authors.affiliation: Institut für Biochemie II, Universität Heidelberg, Germany.
authors.forename: R L
authors.initials: RL
authors.lastname: Krauth-Siegel
authors.forename: C
authors.initials: C
authors.lastname: Sticherling
authors.forename: I
authors.initials: I
authors.lastname: Jöst
authors.forename: C T
authors.initials: CT
authors.lastname: Walsh
authors.forename: E F
authors.initials: EF
authors.lastname: Pai
authors.forename: W
authors.initials: W
authors.lastname: Kabsch
authors.forename: C B
authors.initials: CB
authors.lastname: Lantwin
mesh_terms: D000818:Animals; D003460:Crystallization; D009247:NADH, NADPH Oxidoreductases / Q000037:antagonists & inhibitors / Q000737:chemistry*; D014349:Trypanosoma cruzi / Q000201:enzymology*; D014961:X-Ray Diffraction
chemical_list: D009247:NADH, NADPH Oxidoreductases; C049608:trypanothione reductase