Crystallization and preliminary x-ray characterization of thioredoxin reductase from Escherichia coli.
Single crystals of thioredoxin reductase, suitable for x-ray diffraction studies, have been obtained at room temperature by vapor diffusion of 10-20 mg/ml protein solution against 35% polyethylene glycol containing 200 mM ammonium sulfate. Good quality crystals appear spontaneously only from a protein solution that had been stored for more than a year at 4 degrees C, although large single crystals are reproducibly obtained from fresh protein solutions by micro-seeding. The space group is P6(3)22 (a = b = 123.8 A, c = 81.6 A), with one monomer of the enzyme (34.5 kDa) in the crystallographic asymmetric unit. The crystals are well ordered and diffract to beyond 2 A resolution.
Kuriyan
J
J
Rockefeller University, New York 10021.
Wong
L
L
Russel
M
M
Model
P
P
D003460:Crystallization; D004926:Escherichia coli / Q000201:enzymology*; D009247:NADH, NADPH Oxidoreductases; D011487:Protein Conformation; D013880:Thioredoxin-Disulfide Reductase; D014961:X-Ray Diffraction
D009247:NADH, NADPH Oxidoreductases; D013880:Thioredoxin-Disulfide Reductase