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大肠杆菌水通道蛋白AqpZ的结晶及初步晶体学分析

Crystallization and preliminary crystallographic analysis of the Escherichia coli water channel AqpZ.

作者信息

Daniels Brenda V, Jiang Jian-Sheng, Fu Dax

机构信息

Biology Department, Brookhaven National Laboratory, Upton, NY 11973-5000, USA.

出版信息

Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):561-3. doi: 10.1107/S090744490302972X. Epub 2004 Feb 25.

Abstract

AqpZ is a 24 kDa integral membrane protein that facilitates water movement across the plasma membrane of Escherichia coli. In this study, the first crystallization and preliminary X-ray analysis of AqpZ are described. AqpZ was overexpressed and purified with a yield of 13 mg of purified AqpZ per litre of cell culture. The purified AqpZ was shown to be a monodisperse species consisting of tetrameric protein-detergent complexes. A crystallization condition for producing diffraction-quality crystals was identified. Initial X-ray analysis indicated that the diffraction limit of AqpZ extended to 3.6 A. Crystals were found to belong to space groups P4(1)22 or P4(3)22, with unit-cell parameters a = b = 119.04, c = 380.23 A.

摘要

水通道蛋白Z(AqpZ)是一种24千道尔顿的整合膜蛋白,可促进水穿过大肠杆菌的质膜。在本研究中,描述了AqpZ的首次结晶及初步X射线分析。AqpZ经过量表达和纯化,每升细胞培养物可获得13毫克纯化的AqpZ。纯化的AqpZ显示为一种由四聚体蛋白-去污剂复合物组成的单分散物质。确定了产生衍射质量晶体的结晶条件。初步X射线分析表明,AqpZ的衍射极限延伸至3.6埃。发现晶体属于空间群P4(1)22或P4(3)22,晶胞参数a = b = 119.04,c = 380.23埃。

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