Campus Units

Biochemistry, Biophysics and Molecular Biology, Molecular, Cellular and Developmental Biology, Physics and Astronomy

Document Type

Article

Publication Version

Published Version

Publication Date

2008

Journal or Book Title

Acta Crystallographica Section F

Volume

64

Issue

4

First Page

289

Last Page

292

DOI

10.1107/S1744309108006490

Abstract

The crystallization and preliminary X-ray data analysis of the NorM multidrug efflux pump produced by Neisseria gonorrhoeae are reported. NorM is a cytoplasmic membrane protein that consists of 459 amino-acid residues. It is a member of the recently classified multidrug and toxic compound extrusion (MATE) family of transporters and recognizes a number of cationic toxic compounds such as ethidium bromide, acriflavin, 2-N-methylellipticinium and ciprofloxacin. Recombinant NorM protein was expressed in Escherichia coli and purified by metal-affinity and gel-filtration 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 anisotropically to 3.8 Å and diffraction data were complete to 6.5 Å resolution. The space group was determined to be C2, with unit-cell parameters a = 81.5, b = 164.4, c = 111.5 Å.

Comments

This article is from Acta Crystallographica Section F 64 (2008): 289, doi:10.1107/S1744309108006490. Posted with permission.

Copyright Owner

International Union of Crystallography

Language

en

File Format

application/pdf