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氢化和全氘代大鼠γE-晶状体蛋白在H₂O和D₂O中的精细X射线结构比较。

A comparison of refined X-ray structures of hydrogenated and perdeuterated rat gammaE-crystallin in H2O and D2O.

作者信息

Artero Jean Baptiste, Härtlein Michael, McSweeney Sean, Timmins Peter

机构信息

Institut Laue Langevin, 6 Rue Jules Horowitz, 38042 Grenoble CEDEX 9, France.

出版信息

Acta Crystallogr D Biol Crystallogr. 2005 Nov;61(Pt 11):1541-9. doi: 10.1107/S0907444905028532. Epub 2005 Oct 19.

DOI:10.1107/S0907444905028532
PMID:16239733
Abstract

Rat gammaE-crystallin was overexpressed, purified under different labelling conditions and crystallized and X-ray data were collected at resolutions between 1.71 and 1.36 A. The structures were determined by molecular replacement. In these structures, the cd loop of the Greek-key motif 3, which is the major structural key motif of the two phase-transition groups of gamma-crystallins, presents a double conformation. The influence of the perdeuteration on the protein structure was determined by comparison of the atomic positions and temperature factors of the different models. The perdeuterated proteins have a similar structure to their hydrogenated counterparts, but partial or full deuteration may have some effect on the atomic B-factor values.

摘要

大鼠γE-晶状体蛋白被过表达,在不同标记条件下纯化、结晶,并收集了分辨率在1.71至1.36埃之间的X射线数据。通过分子置换确定结构。在这些结构中,希腊钥匙基序3的cd环呈现出双重构象,希腊钥匙基序3是γ-晶状体蛋白两个相变组的主要结构关键基序。通过比较不同模型的原子位置和温度因子,确定了全氘代对蛋白质结构的影响。全氘代蛋白质与其氢化对应物具有相似的结构,但部分或完全氘代可能对原子B因子值有一些影响。

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