Crystallization and preliminary X-ray diffraction studies of a fungal hydrolase from Ophiostoma novo-ulmi.
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.
Isupov
Michail N
MN
Henry Wellcome Building for Biocatalysis, School of Biological and Chemical Sciences, University of Exeter, Exeter EX4 4QD, England.
Brindley
Amanda A
AA
Hollingsworth
Edward J
EJ
Murshudov
Garib N
GN
Vagin
Alexei A
AA
Littlechild
Jennifer A
JA
D001203:Ascomycota / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D018076:DNA, Complementary / Q000378:metabolism; D004583:Electrons; D004926:Escherichia coli / Q000378:metabolism; D006867:Hydrolases / Q000737:chemistry*; D011487:Protein Conformation; D014961:X-Ray Diffraction / Q000379:methods*
D018076:DNA, Complementary; D006867:Hydrolases