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 analysis of a novel histidinol-phosphate phosphatase from Thermococcus onnurineus NA1
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Crystallization and preliminary X-ray crystallographic analysis of a novel histidinol-phosphate phosphatase from Thermococcus onnurineus NA1

机译:新型嗜热球菌NA1的组氨酸磷酸磷酸酶的结晶和初步X射线晶体学分析

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摘要

The TON_0887 gene product from Thermococcus onnurineus NA1 is a 240-residue protein that has histidinol-phosphate phosphatase (HolPase) activity. According to analysis of its primary structure, the TON_0887 gene product is a monofunctional HolPase that belongs to the DDDD superfamily. This contrasts with the generally accepted classification that bifunctional HolPases belong to the DDDD superfamily. The TON_0887 gene product was purified and crystallized at 295 K. A 2.2 Å resolution data set was collected using synchrotron radiation. The TON-HolPase crystals belonged to space group P2221, with unit-cell parameters a = 40.88, b = 46.89, c = 148.03 Å. Assuming the presence of one molecule in the asymmetric unit, the solvent content was estimated to be about 48.3%.
机译:Onnucoincus NA1的TON_0887基因产物是具有240个残基的蛋白质,具有组蛋白磷酸磷酸酶(HolPase)的活性。根据对其主要结构的分析,TON_0887基因产物是属于DDDD超家族的单功能HolPase。这与公认的双功能HolPases属于DDDD超家族的分类相反。 TON_0887基因产物在295 K纯化并结晶,使用同步加速器辐射收集了2.2Å的分辨率数据集。 TON-HolPase晶体属于空间群P2221,单位晶胞参数a = 40.88,b = 46.89,c = 148.03。假设不对称单元中存在一个分子,则溶剂含量估计为约48.3%。

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