Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the regulator AcrR from Escherichia coli.
Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the regulator AcrR from Escherichia coli.
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大肠杆菌调节因子 AcrR 的克隆、表达、纯化、结晶和初步 X 射线衍射分析。
DOI：
10.1107/s1744309106042576
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发表时间：
2006
期刊：
影响因子：
--
通讯作者：
Yu,EdwardW
中科院分区：
文献类型：
--
作者：
Li,Ming;Qiu,Xi;Su,Chih-Chia;Long,Feng;Gu,Ruoyu;McDermott,Gerry;Yu,EdwardW
This paper describes the cloning, expression, purification and preliminary X-ray data analysis of the AcrR regulatory protein. The Escherichia coli AcrR is a member of the TetR family of transcriptional regulators. It regulates the expression of the AcrAB multidrug transporter. Recombinant AcrR with a 6×His tag at the C-terminus was expressed in E. coli and purified by metal-affinity chromatography. The protein was crystallized using hanging-drop vapor diffusion. X-ray diffraction data were collected from cryocooled crystals at a synchrotron light source. The best crystal diffracted to 2.5 Å. The space group was determined to be P32, with unit-cell parameters a = b = 46.61, c = 166.16 Å.
DOI：
10.1016/s0021-9258(18)46956-6
发表时间：
1994-11
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
M. Ahmed;C. Borsch;S. Taylor;N. Vázquez-Laslop;A. Neyfakh
通讯作者：
M. Ahmed;C. Borsch;S. Taylor;N. Vázquez-Laslop;A. Neyfakh