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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Crystallization and aldo-keto reductase activity of Gcy1p from Saccharomyces cerevisiae
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Crystallization and aldo-keto reductase activity of Gcy1p from Saccharomyces cerevisiae

机译：结晶和aldo-keto还原酶的活动酿酒酵母的Gcy1p

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摘要

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 P2_1, with unit-cell parameters a = 50.94, b = 65.64, c = 86.23 A, β = 92.64 deg. Diffraction data were collected to 2.5 A. Assuming two 35 kDa subunits in the asymmetric unit yielded a V_m of 2.06 A~3 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.
机译：结晶和初步的x射线衍射研究Gcy1p, aldo-keto还原酶酿酒酵母,已执行。野生型和double-mutant形式的使用悬滴Gcy1p是结晶方法在298 K;到目前为止取得了晶体适合形式x射线衍射分析。属于原始的单斜晶体的空间群P2_1,晶胞参数= 50.94,=65.64, c = 86.23,β= 92.64度。衍射2.5数据收集。亚基的不对称单元产生一个V_m2.06 ~ 3哒~(1)。由测量的氧化速度NADPH的几种基质表明,野生型和double-mutant蛋白质酶拥有NADPH-dependent还原酶活性。

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