Crystallization and preliminary X-ray diffraction studies of Gcy1p, an aldo
-keto reductase from Saccharomyces cerevisiae, have been performed. Both th
e wild type and a double-mutant form of Gcy1p were crystallized using the h
anging-drop method at 298 K; however, only the double-mutant form has so fa
r yielded crystals suitable for X-ray diffraction analysis. These crystals
belonged to the primitive monoclinic space group P2(1), with unit-cell para
meters a = 50.94, b = 65.64, c = 86.23 Angstrom, beta = 92.64 degrees. Diff
raction data were collected to 2.5 Angstrom. Assuming two 35 kDa subunits i
n the asymmetric unit yielded a V-m of 2.06 Angstrom(3) Da(-1). Additionall
y, a kinetic study performed by measuring the rate of oxidation of NADPH in
the presence of several substrates indicates that both wild-type and doubl
e-mutant proteins are enzymes possessing NADPH-dependent reductase activity
.