Crystallization and preliminary crystallographic studies of Saccharomyces cerevisiae alcohol dehydrogenase I.
The cytoplasmic yeast alcohol dehydrogenase I crystallized at 5 degrees C as hexagonal plates or short columns in the presence of NAD+ and 2,2,2-trifluoroethanol, in sodium N-tris(hydroxymethyl)methyl-3-aminopropanesulfonate buffer at pH 8.2 to 8.6, using polyethylene glycol 4000 as precipitant. X-ray diffraction data to 3.2 A resolution show that the crystals are hexagonal in space group P622 with unit cell dimensions a = b = 147.9 A, c = 69.1 A. There is one subunit of the tetrameric enzyme per asymmetric unit, giving a packing density of 2.9 A3/Da.
Ramaswamy
S
S
Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala.
Kratzer
D A
DA
Hershey
A D
AD
Rogers
P H
PH
Arnone
A
A
Eklund
H
H
Plapp
B V
BV
D000426:Alcohol Dehydrogenase / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D000426:Alcohol Dehydrogenase