Campus Units

Biochemistry, Biophysics and Molecular Biology, Physics and Astronomy

Document Type

Article

Publication Version

Published Version

Publication Date

2006

Journal or Book Title

Acta Crystallographica Section F

Volume

62

Issue

11

First Page

1150

Last Page

1152

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.

Comments

This article is from Acta Crystallographica Section F 62 (2006): 1150, doi:10.1107/S1744309106042576. Posted with permission.

Copyright Owner

International Union of Crystallography

Language

en

File Format

application/pdf

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