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来自大肠杆菌的C端TonB片段的结晶及初步X射线分析

Crystallization and preliminary X-ray analysis of a C-terminal TonB fragment from Escherichia coli.

作者信息

Koedding Jiri, Polzer Patrick, Killig Frank, Howard S Peter, Gerber Kinga, Seige Peter, Diederichs Kay, Welte Wolfram

机构信息

Department of Biology, University of Konstanz, 78457 Konstanz, Germany.

出版信息

Acta Crystallogr D Biol Crystallogr. 2004 Jul;60(Pt 7):1281-3. doi: 10.1107/S0907444904009722. Epub 2004 Jun 22.

DOI:10.1107/S0907444904009722
PMID:15213392
Abstract

The TonB protein located in the cell wall of Gram-negative bacteria mediates the proton motive force from the cytoplasmic membrane to specific outer membrane transporters. A C-terminal fragment of TonB from Escherichia coli consisting of amino-acid residues 147-239 (TonB-92) has been purified and crystallized. Crystals grew in space group P2(1) to dimensions of about 1.0 x 0.12 x 0.12 mm. A native data set has been obtained to 1.09 A resolution.

摘要

位于革兰氏阴性菌细胞壁中的TonB蛋白介导了质子动力从细胞质膜到特定外膜转运蛋白的传递。来自大肠杆菌的TonB的C末端片段(由氨基酸残基147 - 239组成,即TonB - 92)已被纯化并结晶。晶体生长于空间群P2(1),尺寸约为1.0×0.12×0.12毫米。已获得分辨率为1.09埃的天然数据集。

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