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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Cloning, purification, crystallization and preliminary X-ray analysis of DOS heme domain, a new heme oxygen sensor in Escherichia coli.
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Cloning, purification, crystallization and preliminary X-ray analysis of DOS heme domain, a new heme oxygen sensor in Escherichia coli.

机译:克隆、纯化、结晶初步的x射线分析DOS血红素域,大肠杆菌的新血红素氧传感器。

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摘要

The heme-containing PAS domain of the direct oxygen-sensor protein (DOS(H)), a bona fide oxygen-sensor protein, has been cloned from Escherichia coli strain K12 and successfully purified. The oxidized form of this protein was crystallized by the hanging-drop method with a PEG 8000-based precipitant. Preliminary X-ray diffraction studies of the PAS-domain crystal show that it belongs to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 46.1, b = 68.1, c = 82.6 A. A complete diffraction data set was collected to 1.9 A for MAD phasing. The electron-density map shows two molecules in an asymmetric unit and a unique six-coordination of the heme iron.
机译:heme-containing不是域的直接氧传感器的蛋白质(DOS (H)),一个善意的氧传感器蛋白,克隆大肠杆菌菌株K12的和成功的净化。悬滴结晶的方法基于8000年的沉淀剂挂钩。PAS-domain晶体的衍射研究表明它属于斜方晶系的空间集团P2(1) 2(1) 2(1),晶胞参数= 46.1, b = 68.1, c = 82.6。衍射数据集收集1.9疯狂的定相。在不对称单位和一个独特的分子six-coordination的血红素铁。

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