Purification, crystallization and preliminary X-ray studies of GMP reductase 2 from human.

Ji CN; Ying G; Deng YFChen SZhang WHShu GXie YMao YM

首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Purification, crystallization and preliminary X-ray studies of GMP reductase 2 from human.

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Purification, crystallization and preliminary X-ray studies of GMP reductase 2 from human.

机译：净化、结晶和初步的从人类x射线研究GMP还原酶2。

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GMP reductase 2 from human has been expressed in Escherichia coli, purified and crystallized. The crystals belong to space group P3(2)21, with unit-cell parameters a = b = 110.6, c = 209.8 A, alpha = beta = 90, gamma = 120 degrees. Diffraction data were collected to 3.0 A with a completeness of 100% (100% for the last shell), an R(merge) value of 0.089 (0.189) and an I/sigma(I) value of 7.3 (3.2).

机译：GMP还原酶2从人类中表达大肠杆菌、纯化和结晶。水晶属于空间群P3(2) 21日晶胞参数a = b = 110.6, c = 209.8,α=β= 90,γ= 120度。衍射数据收集与一个3.0去年壳牌完整性的100% (100%),R(合并)0.089(0.189)和一个值我/σ(I) 7.3(3.2)的价值。

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《Acta crystallographica.Section D. Biological crystallography》 |2003年第6期|1109-1110|共2页
作者
Ji CN; Ying G; Deng YFChen SZhang WHShu GXie YMao YM;
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作者单位

State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Sciences, Fudan University, Shanghai 200433, People's Republic of China.;

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正文语种英语
中图分类化学;
关键词
Human; completeness; PurificationcrystalsX-raysCrystallization;

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Purification, crystallization and preliminary X-ray studies of GMP reductase 2 from human.

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