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Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the regulator AcrR from Escherichia coli

Journal Article · · Acta Crystallographica. Section F
 [1];  [2];  [3];  [4];  [1];  [5]
  1. Department of Physics and Astronomy, Iowa State University, Ames, IA 50011 (United States)
  2. Interdepartmental Genetics Graduate Program, Iowa State University, Ames, IA 50011 (United States)
  3. Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011 (United States)
  4. Molecular, Cellular and Developmental Biology Interdepartmental Graduate Program, Iowa State University, Ames, IA 50011 (United States)
  5. 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