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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Purification, crystallization and preliminary X-ray diffraction studies of a Ca2+-binding protein, human S100P.
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Purification, crystallization and preliminary X-ray diffraction studies of a Ca2+-binding protein, human S100P.

机译:净化、结晶和初步的x射线衍射研究Ca2 +绑定人类S100P蛋白质,。

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摘要

S100P, a Ca(2+)-binding protein, is a member of the S100 family. Its presence is associated with the development of prostate cancer, but its cellular function is not known. Recombinant human S100P has been expressed and purified in bacterial cells and crystals of human S100P in the calcium-bound state have been grown using the vapour-diffusion technique with PEG 4000 as precipitant. Diffraction data have been obtained to a resolution of 2.0 A from a single frozen S100P crystal which belongs to the space group P4(1)2(1)2, with unit-cell parameters a = b = 60.8, c = 47.6 A.
机译:S100P Ca(2 +)结合蛋白,属于S100家族。前列腺癌的发展,但是它的细胞功能尚不清楚。S100P一直在表达和纯化细菌细胞和人类S100P晶体calcium-bound状态已被使用vapour-diffusion技术与4000年挂钩沉淀剂。2.0的决议从单一冻结S100P晶体属于空间群P4(1) 2(1) 2,晶胞参数a = b =60.8, c = 47.6。

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