title: Crystallization and preliminary X-ray diffraction analysis of the multidrug efflux transporter NorM from Neisseria gonorrhoeae.
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 A and diffraction data were complete to 6.5 A resolution. The space group was determined to be C2, with unit-cell parameters a = 81.5, b = 164.4, c = 111.5 A.
authors.affiliation: Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011, USA.
authors.forename: Chih-Chia
authors.initials: CC
authors.lastname: Su
authors.forename: Feng
authors.initials: F
authors.lastname: Long
authors.forename: Gerry
authors.initials: G
authors.lastname: McDermott
authors.forename: William M
authors.initials: WM
authors.lastname: Shafer
authors.forename: Edward W
authors.initials: EW
authors.lastname: Yu
mesh_terms: D000595:Amino Acid Sequence; D017920:Antiporters / Q000032:analysis / Q000737:chemistry* / Q000235:genetics; D001426:Bacterial Proteins / Q000032:analysis / Q000737:chemistry* / Q000235:genetics; D003460:Crystallization; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D009344:Neisseria gonorrhoeae / Q000737:chemistry* / Q000235:genetics
chemical_list: D017920:Antiporters; D001426:Bacterial Proteins; C114619:NorM protein, bacteria