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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Purification and crystallization of a novel membrane-anchored protein: the Schistosoma haematobium serpin.
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Purification and crystallization of a novel membrane-anchored protein: the Schistosoma haematobium serpin.

机译:纯化和结晶的小说membrane-anchored蛋白质:血吸虫

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摘要

A unique serine-protease inhibitor (serpin) of the blood fluke S. haematobium has been crystallized. It is an antitrypsin with an unusual residue (phenylalanine) at its reactive center. Unlike any known member of this gene family, it is a membrane-anchored protein on the surface of the parasite. The location of this serpin and immunological response to the protein indicate that it may play a important role in host-parasite interaction. The crystals belong to the trigonal space group P3221 or P3121 with unit-cell parameters a = b = 64.7, c = 186.7 A, alpha = 90.0, beta = 90.0, gamma = 120.0 degrees. There is one molecule per asymmetric unit and the crystals diffracted to 2.2 A.
机译:一个独特的丝氨酸蛋白酶抑制剂(serpin)血吸虫的埃及血吸虫结晶。它是一个抗胰蛋白酶与一个不寻常的残渣(苯丙氨酸)在其活性中心。任何已知的这个基因家族的成员,这是一个membrane-anchored蛋白质表面的寄生虫。免疫反应的蛋白质它可能会发挥重要的作用开始互动。三方晶系的空间组P3221或P3121晶胞参数a = b = 64.7, c = 186.7,α= 90.0,β= 90.0,γ= 120.0度。有一个每单元和不对称分子2.2晶体衍射。

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