Related Experiment Video
Updated: Jul 19, 2026
Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD
Published on: December 30, 2016
Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the regulator AcrR
Ming Li1, Xi Qiu, Chih-Chia Su
1Department of Physics and Astronomy, Iowa State University, Ames, IA 50011, USA.
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 6xHis 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 A. The space group was determined to be P3(2), with unit-cell parameters a = b = 46.61, c = 166.16 A.
