Abstract
Crystallization and preliminary X-ray diffraction studies of Gcy1p, an aldo-keto reductase from Saccharomyces cerevisiae, have been performed. Both the wild type and a double-mutant form of Gcy1p were crystallized using the hanging-drop method at 298 K; however, only the double-mutant form has so far yielded crystals suitable for X-ray diffraction analysis. These crystals belonged to the primitive monoclinic space group P21, with unit-cell parameters a = 50.94, b = 65.64, c = 86.23 Å, β = 92.64°. Diffraction data were collected to 2.5 Å. Assuming two 35 kDa subunits in the asymmetric unit yielded a V(m) of 2.06 Å3 Da-1. Additionally, a kinetic study performed by measuring the rate of oxidation of NADPH in the presence of several substrates indicates that both wild-type and double-mutant proteins are enzymes possessing NADPH-dependent reductase activity.
Original language | English (US) |
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Pages (from-to) | 763-765 |
Number of pages | 3 |
Journal | Acta Crystallographica Section D: Biological Crystallography |
Volume | 56 |
Issue number | 6 |
DOIs | |
State | Published - 2000 |
ASJC Scopus subject areas
- Clinical Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biophysics
- Condensed Matter Physics
- Structural Biology