Initiating a crystallographic study of trypanothione reductase.
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.
Hunter
W N
WN
Department of Chemistry, University of Manchester, U.K.
Smith
K
K
Derewenda
Z
Z
Harrop
S J
SJ
Habash
J
J
Islam
M S
MS
Helliwell
J R
JR
Fairlamb
A H
AH
D000818:Animals; D003421:Crithidia / Q000201:enzymology; D003460:Crystallization; D009247:NADH, NADPH Oxidoreductases / Q000737:chemistry* / Q000302:isolation & purification; D014961:X-Ray Diffraction
D009247:NADH, NADPH Oxidoreductases; C049608:trypanothione reductase