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Article
Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the regulator AcrR from Escherichia coli
Acta Crystallographica Section F
Document Type
Article
Publication Version
Published Version
Publication Date
1-1-2006
DOI
10.1107/S1744309106042576
Abstract
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.
Copyright Owner
International Union of Crystallography
Copyright Date
2006
Language
en
File Format
application/pdf
Citation Information
Ming Li, Xi Qiu, Chih-Chia Su, Feng Long, et al.. "Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the regulator AcrR from Escherichia coli" Acta Crystallographica Section F Vol. 62 Iss. 11 (2006) p. 1150 - 1152 Available at: http://works.bepress.com/edward_yu/8/
This article is from Acta Crystallographica Section F 62 (2006): 1150, doi:10.1107/S1744309106042576. Posted with permission.