Open AccessCrystallization and preliminary X‐ray diffraction analysis of the multidrug efflux transporter NorM from Neisseria gonorrhoeae
Author(s) -
Su ChihChia,
Long Feng,
McDermott Gerry,
Shafer William M.,
Yu Edward W.
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108006490
Subject(s) - efflux , neisseria gonorrhoeae , crystallization , ethidium bromide , escherichia coli , chemistry , chromatography , biology , biochemistry , microbiology and biotechnology , organic chemistry , gene , dna
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 C 2, with unit‐cell parameters a = 81.5, b = 164.4, c = 111.5 Å.