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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Purification, crystallization and preliminary X-ray diffraction analysis of the yeast phosphorelay protein YPD1.
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Purification, crystallization and preliminary X-ray diffraction analysis of the yeast phosphorelay protein YPD1.

机译:净化、结晶和初步的x射线衍射分析酵母YPD1 phosphorelay蛋白质。

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摘要

YPD1 is a yeast osmoregulatory protein that functions in a phosphorelay signal-transduction pathway. YPD1 has been expressed in Escherichia coli, purified to homogeneity and crystallized. The crystals were obtained by hanging-drop vapor-diffusion using PEG 4000 as a precipitant. Preliminary X-ray diffraction analysis indicates that the crystals belong to tetragonal space group P43212 or P41212 with unit-cell dimensions a = b = 52.71, c = 244.02 A. X-ray data to 2.7 and 3.0 A have been collected from native crystals and a heavy-atom derivative, respectively. Positions for two Hg atoms have been located by analysis of difference Patterson maps.
机译:YPD1酵母渗透调节的蛋白质函数在一个phosphorelay信号转导途径。杆菌、纯化同质性和结晶。晶体是通过悬滴扩散使用挂钩4000作为沉淀剂。初步的x射线衍射分析表明水晶属于正方的空间集团P43212或P41212单胞尺寸a = b = 52.71, c = 244.02。和3.0已经收集了从本地水晶和重原子衍生物,分别。被分析位于帕特森的区别地图。

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