title: Preliminary crystallographic analysis of trypanothione reductase from Crithidia fasciculata.
abstract: 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.
authors.affiliation: Laboratory of Molecular Biophysics, Rockefeller University, New York, NY 10021.
authors.forename: J
authors.initials: J
authors.lastname: Kuriyan
authors.forename: L
authors.initials: L
authors.lastname: Wong
authors.forename: B D
authors.initials: BD
authors.lastname: Guenther
authors.forename: N J
authors.initials: NJ
authors.lastname: Murgolo
authors.forename: A
authors.initials: A
authors.lastname: Cerami
authors.forename: G B
authors.initials: GB
authors.lastname: Henderson
mesh_terms: D000818:Animals; D003421:Crithidia / Q000201:enzymology*; D009247:NADH, NADPH Oxidoreductases / Q000737:chemistry*; D014961:X-Ray Diffraction
chemical_list: D009247:NADH, NADPH Oxidoreductases; C049608:trypanothione reductase