Preliminary crystallographic analysis of the antibiotic discharge outer membrane lipoprotein OprM of Pseudomonas aeruginosa with an exceptionally long unit cell and complex lattice structure
- Department of Molecular Life Science, Tokai University School of Medicine, Isehara 259-1193 (Japan)
- The Institute for Protein Research, Osaka University, Suita 565-0871 (Japan)
The OprM subunit of the MexAB-OprM efflux pump in P. aeruginosa is an outer membrane-anchored lipoprotein. OprM crystals have been grown at 293 K in the presence of 2-methyl-2,4-propanediol and a combination of surfactants and diffracted to 2.56 Å resolution. Crystals of the drug-discharge outer membrane protein OprM (MW = 50.9 kDa) of the MexAB-OprM multidrug transporter of Pseudomonas aeruginosa have been grown at 293 K in the presence of 2-methyl-2,4-propanediol and a combination of surfactants. The crystal belonged to space group R32, with unit-cell parameters a = b = 85.43, c = 1044.3 Å. Diffraction data for OprM were obtained using the undulator synchrotron-radiation beamline at SPring-8 (BL44XU, Osaka University), which allowed an extra-long specimen-to-detector distance with a wide detector area. The crystal diffracted to 2.56 Å resolution using 0.9 Å X-rays from the synchrotron-radiation source. A heavy-atom derivative for isomorphous replacement phasing was obtained using iridium chloride.
- OSTI ID:
- 22356069
- Journal Information:
- Acta Crystallographica. Section F, Vol. 61, Issue Pt 1; Other Information: PMCID: PMC1952377; PMID: 16508113; PUBLISHER-ID: bw5071; OAI: oai:pubmedcentral.nih.gov:1952377; Copyright (c) International Union of Crystallography 2005; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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