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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Crystallization of the N-terminal domain of human sex hormone-binding globulin, the major sex steroid carrier in blood.
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Crystallization of the N-terminal domain of human sex hormone-binding globulin, the major sex steroid carrier in blood.

机译:结晶的n端结构域的人类性hormone-binding球蛋白,主要性类固醇载体的血液。

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摘要

The amino-teminal laminin G-like domain of human sex hormone-binding globulin (SHBG), which contains the steroid-binding site and the dimerization domain, has been produced in Escherichia coli, purified to homogeneity and crystallized in complex with 5alpha--dihydrotestosterone (DHT) in two different crystal forms. Native data sets have been collected for tetragonal crystals (space group P4(1)22 or P4(3)22; unit-cell parameters a = 52.2, c = 148.4 A) diffracting to 3.3 A and trigonal crystals (R32; a = 104.0, c = 84.4 A) diffracting to better than 1.6 A. Since both crystal forms can only accommodate a single monomer in the asymmetric unit and share twofold rotational symmetry, it is proposed that the homodimer of this truncated form of SHBG, as observed in ultracentrifugation experiments, displays C(2) point-group symmetry.
机译:的amino-teminal层粘连蛋白G-like域的人类性hormone-binding球蛋白,含有类固醇结合网站和二聚作用域,已经生产的大肠杆菌、纯化和同质性在复杂的结晶5α-二氢睾酮(DHT)两种不同的晶体形式。收集了正方晶体(空间组P4(1) 22或P4 (3) 22;= 52.2, c = 148.4和3.3)中三方晶系的晶体(R32;衍射比1.6更好。只能容纳单个晶体形式单体的不对称单元和双重的分享旋转对称,提出为截短形式的SHBG的观察到在超速离心法实验中,显示C(2)对称点群。

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