Open AccessPreliminary crystallographic analysis of the antibiotic discharge outer membrane lipoprotein OprM of Pseudomonas aeruginosa with an exceptionally long unit cell and complex lattice structure
Author(s) -
Akama Hiroyuki,
Kanemaki Misa,
Tsukihara Tomitake,
Nakagawa Atsushi,
Nakae Taiji
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309104031914
Subject(s) - beamline , crystal structure , crystallography , materials science , synchrotron radiation , diffraction , chemistry , physics , optics , beam (structure)
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 R 32, 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.