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首页> 外文期刊>Acta crystallographica. Section F, Structural biology communications >Crystallization and preliminary X-ray crystallographic analysis of human myotubularin-related protein 1
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Crystallization and preliminary X-ray crystallographic analysis of human myotubularin-related protein 1

机译:人肌管蛋白相关蛋白1的结晶和初步X射线晶体学分析

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摘要

Myotubularin-related protein 1 is a phosphatase that dephosphorylates phospholipids such as phosphatidylinositol 3-phosphate or phosphatidylinositol 3,5-bisphosphate. In this study, human MTMR1 was overexpressed in Escherichia coli, purified and crystallized at 277 K using polyethylene glycol 20 000 as a precipitant. Diffraction data were collected to 2.0 angstrom resolution using synchrotron radiation. The crystals belonged to space group P1, with unit-cell parameters a = 67.219, b = 96.587, c = 97.581 angstrom, alpha = 87.597, beta = 86.072, gamma = 77.327 degrees. Assuming the presence of four molecules in the asymmetric unit, the calculated Matthews coefficient value was 2.61 angstrom 3 Da(-1) and the corresponding solvent content was 52.9%.
机译:肌管蛋白相关蛋白1是使磷脂(例如磷脂酰肌醇3-磷酸酯或磷脂酰肌醇3,5-双磷酸酯)去磷酸化的磷酸酶。在这项研究中,人类MTMR1在大肠杆菌中过表达,使用20,000聚乙二醇作为沉淀剂在277 K纯化和结晶。使用同步加速器辐射将衍射数据收集到2.0埃分辨率。晶体属于空间群P1,其晶胞参数a = 67.219,b = 96.587,c = 97.581埃,α= 87.597,β= 86.072,γ= 77.327度。假设在不对称单元中存在四个分子,则计算出的马修斯系数值为2.61埃3 Da(-1),相应的溶剂含量为52.9%。

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