Crystallization and preliminary crystallographic analysis of trypanothione reductase from Trypanosoma cruzi, the causative agent of Chagas' disease.
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.
Krauth-Siegel
R L
RL
Institut für Biochemie II, Universität Heidelberg, Germany.
Sticherling
C
C
Jöst
I
I
Walsh
C T
CT
Pai
E F
EF
Kabsch
W
W
Lantwin
C B
CB
D000818:Animals; D003460:Crystallization; D009247:NADH, NADPH Oxidoreductases / Q000037:antagonists & inhibitors / Q000737:chemistry*; D014349:Trypanosoma cruzi / Q000201:enzymology*; D014961:X-Ray Diffraction
D009247:NADH, NADPH Oxidoreductases; C049608:trypanothione reductase