Crystallization and rhenium MAD phasing of the acyl-homoserinelactone synthase EsaI

W. T. Watson, F. V. Murphy IV, T. A. Gould, P. Jambeck, D. L. Val, Jr Cronan, S. B. Von Bodman, M. E.A. Churchill

Research output: Contribution to journalArticlepeer-review


Acyl-homoserine-L-lactones (AHLs) are diffusible chemical signals that are required for virulence of many Gram-negative bacteria. AHLs are produced by AHL synthases from two substrates, S-adenosyl-L-methionine and acyl-acyl carrier protein. The AHL synthase EsaI, which is homologous to the AHL synthases from other pathogenic bacterial species, has been crystallized in the primitive tetragonal space group P43, with unit-cell parameters a = b = 66.40, c = 47.33 Å. The structure was solved by multiple-wavelength anomalous diffraction with a novel use of the rhenium anomalous signal. The rhenium-containing structure has been refined to a resolution of 2.5 Å and the perrhenate ion binding sites and liganding residues have been identified.

Original languageEnglish (US)
Pages (from-to)1945-1949
Number of pages5
JournalActa Crystallographica Section D: Biological Crystallography
Issue number12
StatePublished - 2001
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology


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