Preliminary crystallographic analysis of the antibiotic discharge outer membrane lipoprotein OprM of Pseudomonas aeruginosa with an exceptionally long unit cell and complex lattice structure

被引:1
作者
Akama, H
Kanemaki, M
Tsukihara, T
Nakagawa, A
Nakae, T [1 ]
机构
[1] Tokai Univ, Sch Med, Dept Mol Life Sci, Isehara, Kanagawa 2591193, Japan
[2] Osaka Univ, Inst Prot Res, Suita, Osaka 5650871, Japan
来源
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2005年 / 61卷
关键词
D O I
10.1107/S1744309104031914
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
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 angstrom. 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 angstrom resolution using 0.9 angstrom X-rays from the synchrotron-radiation source. A heavy-atom derivative for isomorphous replacement phasing was obtained using iridium chloride.
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页码:131 / 133
页数:3
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