Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the regulator AcrR from Escherichia coli
Journal Article
·
· Acta Crystallographica. Section F
- Department of Physics and Astronomy, Iowa State University, Ames, IA 50011 (United States)
- Interdepartmental Genetics Graduate Program, Iowa State University, Ames, IA 50011 (United States)
- Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011 (United States)
- Molecular, Cellular and Developmental Biology Interdepartmental Graduate Program, Iowa State University, Ames, IA 50011 (United States)
- Department of Anatomy, School of Medicine, University of California, San Francisco, CA 94143 (United States)
The transcriptional regulator AcrR from Escherichia coli has been cloned, overexpressed, purified and crystallized and X-ray diffraction data have been collected to a resolution of 2.5 Å. 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 P3{sub 2}, with unit-cell parameters a = b = 46.61, c = 166.16 Å.
- OSTI ID:
- 22356401
- Journal Information:
- Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 11 Vol. 62; ISSN ACSFCL; ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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