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 Lon from Thermococcus onnurineus NA1
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Crystallization and preliminary X-ray crystallographic analysis of Lon from Thermococcus onnurineus NA1

机译:洋葱嗜热球菌NA1中Lon的结晶和初步X射线晶体学分析

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摘要

Lon is an oligomeric ATP-dependent protease that degrades defective or denatured proteins as well as some folded proteins for the control of cellular protein quality and metabolism. Lon from Thermococcus onnurineus NA1 was purified and crystallized at 295 K. A 2.0 Å resolution data set was collected using synchrotron radiation. The crystals belonged to space group P63, with unit-cell parameters a = 121.45, b = 121.45, c = 195.24 Å. Assuming the presence of two monomers in the asymmetric unit, the solvent content was estimated to be about 60.7%.
机译:Lon是一种寡聚ATP依赖性蛋白酶,可降解有缺陷或变性的蛋白质以及一些折叠的蛋白质,以控制细胞蛋白质的质量和代谢。纯化并在295 K下结晶来自温热球菌NA1的离子,使用同步加速器辐射收集了2.0Å的分辨率数据集。晶体属于空间群P63,单位晶胞参数a = 121.45,b = 121.45,c = 195.24。假设在不对称单元中存在两种单体,则溶剂含量估计为约60.7%。

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