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Crystallization and preliminary crystallographic studies of Saccharomyces cerevisiae alcohol dehydrogenase I
S Ramaswamy1, D A Kratzer, A D Hershey
1Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala.
Journal of Molecular Biology
|January 14, 1994
Abstract:
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.