title: Initiating a crystallographic study of trypanothione reductase.
abstract: We have obtained well-ordered single crystals of the flavoenzyme trypanothione reductase from Crithidia fasciculata. The crystals are tetragonal rods with unit cell dimensions a = 128.6 A, c = 92.5 A. The diffraction pattern corresponds to a primitive lattice. Laue class 4/m. Diffraction to better than 2.4 A has been recorded at the Daresbury Synchrotron. The accurate elucidation of the three-dimensional structure of this enzyme is required to support the rational design of compounds active against a variety of tropical diseases caused by trypanosomal parasites.
authors: Department of Chemistry, University of Manchester, U.K.
authors: W N
authors: WN
authors: Hunter
authors: K
authors: K
authors: Smith
authors: Z
authors: Z
authors: Derewenda
authors: S J
authors: SJ
authors: Harrop
authors: J
authors: J
authors: Habash
authors: M S
authors: MS
authors: Islam
authors: J R
authors: JR
authors: Helliwell
authors: A H
authors: AH
authors: Fairlamb
mesh_terms: D000818:Animals; D003421:Crithidia / Q000201:enzymology; D003460:Crystallization; D009247:NADH, NADPH Oxidoreductases / Q000737:chemistry* / Q000302:isolation & purification; D014961:X-Ray Diffraction
chemical_list: D009247:NADH, NADPH Oxidoreductases; C049608:trypanothione reductase