Crystallization and preliminary X-ray diffraction studies of a fungal hydrolase from Ophiostoma novo-ulmi

Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1879-82. doi: 10.1107/S0907444904018153. Epub 2004 Sep 23.

Abstract

Dutch elm disease fungus Ophiostoma novo-ulmi contains a hydrolase activity which catalyses the resolution of racemic ethyl naproxen to the corresponding acid. The recombinant enzyme has been crystallized by the vapour-diffusion method in two crystal forms. The crystals of the first form belong to space group P2(1)2(1)2, with unit-cell parameters a = 115.9, b = 174.4, c = 62.1 A. The enzyme also crystallizes in space group P2(1)2(1)2, with unit-cell parameters a = 72.9, b = 212.7, c = 61.7 A. Synchrotron data have been collected for both crystal forms to 2.6 and 2.3 A, respectively. A molecular-replacement solution has been found using a remote starting model of a bacterial esterase (23% sequence identity) for both crystal forms. Multicrystal averaging has resulted in interpretable electron-density maps.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Ascomycota / enzymology*
  • Crystallization
  • Crystallography, X-Ray
  • DNA, Complementary / metabolism
  • Electrons
  • Escherichia coli / metabolism
  • Hydrolases / chemistry*
  • Protein Conformation
  • X-Ray Diffraction / methods*

Substances

  • DNA, Complementary
  • Hydrolases