Crystallization and preliminary diffraction studies of hydroxypyruvate reductase (D-glycerate dehydrogenase) from Hyphomicrobium methylovorum.
Two crystal forms of hydroxypyruvate reductase (D-glycerate dehydrogenase) from the methylotrophic bacterium Hyphomicrobium methylovorum have been grown from ammonium sulphate solutions. One crystal form is triclinic, with unit cell parameters a = 60.4 A, b = 60.5 A, c = 66.3 A, alpha = 102.3 degrees, beta = 113.7 degrees and gamma = 102.7 degrees, suggesting that a dimer (monomer M(r) 38,000) occupies the unit cell. This crystal form diffracts to beyond 2.4 A resolution and is suitable for crystallographic structure analysis.
Goldberg
J D
JD
Imperial College, London, U.K.
Brick
P
P
Yoshida
T
T
Mitsunaga
T
T
Oshiro
T
T
Shimao
M
M
Izumi
Y
Y
D000429:Alcohol Oxidoreductases / Q000737:chemistry* / Q000648:ultrastructure; D001419:Bacteria / Q000201:enzymology; D003461:Crystallography; D050537:Hydroxypyruvate Reductase; D014961:X-Ray Diffraction
D000429:Alcohol Oxidoreductases; D050537:Hydroxypyruvate Reductase