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

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Hiroyuki AkamaTaiji Nakae

Abstract

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 A. 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 A resolution using 0.9 A X-rays from the synchrotron-radiation source. A heavy-atom derivative for isomorphous replacement phasing was obtained using iridium chloride.

References

Oct 11, 2002·Nature·Satoshi MurakamiAkihito Yamaguchi
Apr 28, 2004·FEBS Letters·Klaas M PosKay Diederichs
May 1, 2004·The Journal of Biological Chemistry·Hiroyuki AkamaTaiji Nakae
Jul 1, 2004·Proceedings of the National Academy of Sciences of the United States of America·Matthew K HigginsVassilis Koronakis

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