首页> 美国卫生研究院文献>Acta Crystallographica Section F: Structural Biology and Crystallization Communications >Crystallization and preliminary X-ray crystallographic study of NiFe-hydrogenase maturation factor HypE from Thermococcus kodakaraensis KOD1
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Crystallization and preliminary X-ray crystallographic study of NiFe-hydrogenase maturation factor HypE from Thermococcus kodakaraensis KOD1

机译:柯达热球菌KOD1中NiFe-加氢酶成熟因子HypE的结晶及初步X射线晶体学研究

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摘要

The hydrogenase maturation protein HypE is involved in the biosynthesis of the CN ligands of the active-site iron of [NiFe] hydrogenases using carbamoylphosphate as a substrate. Here, the crystallization and preliminary crystallographic analysis of HypE from Thermococcus kodakaraensis KOD1 are reported. Crystals of HypE (338 amino acids, 35.9 kDa) have been obtained by the sitting-drop vapour-diffusion method using 2-methyl-2,4-pentanediol (MPD) as a precipitant. The crystals belong to space group P21212, with unit-cell parameters a = 88.3, b = 45.8, c = 75.1 Å. There is one HypE molecule in the asymmetric unit. A complete native X-ray diffraction data set was collected to a maximum resolution of 1.55 Å at 100 K.
机译:氢化酶成熟蛋白HypE以氨基甲酸酯磷酸酯为底物参与[NiFe]氢化酶活性位铁的CN配体的生物合成。在此,报道了来自柯达热球菌KOD1的HypE的结晶和初步晶体学分析。 HypE(338个氨基酸,35.9kk)的晶体已经通过坐滴气相扩散法使用2-甲基-2,4-戊二醇(MPD)作为沉淀剂获得。晶体属于空间群P21212,单位晶胞参数a = 88.3,b = 45.8,c = 75.1。不对称单元中有一个HypE分子。完整的原始X射线衍射数据集在100 K时的最大分辨率为1.55Å。

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