Crystallization and preliminary X-ray diffraction analysis of the multidrug efflux transporter NorM from Neisseria gonorrhoeae

Journal Article · Tue Jun 03 04:00:00 EDT 2008 · Acta Crystallogr. F

DOI:https://doi.org/10.1107/S1744309108006490· OSTI ID:1006619

Su, C C; Long, F; McDermott, G; Shafer, W M; Yu, E W ^[1]

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1. Emory-MED

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 {angstrom} and diffraction data were complete to 6.5 {angstrom} resolution. The space group was determined to be C2, with unit-cell parameters a = 81.5, b = 164.4, c = 111.5 {angstrom}.

• Research Organization: Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)
• Sponsoring Organization: USDOE
• OSTI ID: 1006619
• Journal Information: Acta Crystallogr. F, Journal Name: Acta Crystallogr. F Journal Issue: (4) ; 04, 2008 Vol. 64; ISSN 1744-3091
• Country of Publication: United States
• Language: ENGLISH

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
60 APPLIED LIFE SCIENCES
AMINO ACIDS
CHROMATOGRAPHY
CRYSTALLIZATION
CRYSTALS
DATA ANALYSIS
DIFFRACTION
DIFFUSION
ESCHERICHIA COLI
EXTRUSION
MEMBRANE PROTEINS
PROTEINS
RESIDUES
RESOLUTION
SPACE GROUPS
X-RAY DIFFRACTION