Preliminary crystallographic analysis of trypanothione reductase from Crithidia fasciculata.
Trypanothione reductase, a flavoprotein disulfide reductase specific to trypanosomatid parasites, has been crystallized by vapor diffusion of a protein solution (10 mg/ml) against 22% polyethylene glycol (average Mr 8000) containing 100 mM-ammonium sulfate. Crystals of a size suitable for structure determination by X-ray diffraction have been obtained by seeding protein solutions with smaller crystals. The space-group is P21 (a = 60.9 A, b = 161.8 A, c = 58.4 A, beta = 99.1 degrees). The molecular mass and volume of the unit cell suggest that there is a dimer of the enzyme in the asymmetric unit, and this is confirmed by self-rotation functions calculated using data to 4.5 A resolution. The crystals diffract to beyond 3 A resolution. Crystals of another P21 form (a = 91.3 A, b = 114.4 A, c = 92.0 A, beta = 141.3 degrees) are observed to grow under similar conditions.
Kuriyan
J
J
Laboratory of Molecular Biophysics, Rockefeller University, New York, NY 10021.
Wong
L
L
Guenther
B D
BD
Murgolo
N J
NJ
Cerami
A
A
Henderson
G B
GB
D000818:Animals; D003421:Crithidia / Q000201:enzymology*; D009247:NADH, NADPH Oxidoreductases / Q000737:chemistry*; D014961:X-Ray Diffraction
D009247:NADH, NADPH Oxidoreductases; C049608:trypanothione reductase