Crystallization and preliminary X-ray analysis of the flavoenzyme vanillyl-alcohol oxidase from Penicillium simplicissimum.
Vanillyl-alcohol oxidase catalyses the oxidation of several 4-hydroxybenzyl alcohols by using 8-alpha-(N3-histidyl)-FAD as a covalently bound prosthetic group. Crystals of vanillyl-alcohol oxidase from Penicillium simplicissimum have been grown by using the vapor diffusion technique. The space group was found to be I, with cell dimensions a = b = 140.5 A, c = 132.9 A. Diffraction data have been recorded to 3.2 A resolution by using a laboratory source and to 2.5 A resolution on flash freezing the crystal at the ELETTRA Synchrotron X-ray diffraction beam line.
Mattevi
A
A
Department of Genetics and Microbiology, University of Pavia, Italy.
Fraaije
M W
MW
Coda
A
A
van Berkel
W J
WJ
D000429:Alcohol Oxidoreductases / Q000737:chemistry*; D018360:Crystallography, X-Ray; D005182:Flavin-Adenine Dinucleotide / Q000737:chemistry; D005420:Flavoproteins / Q000737:chemistry*; D010407:Penicillium / Q000201:enzymology*
D005420:Flavoproteins; D005182:Flavin-Adenine Dinucleotide; D000429:Alcohol Oxidoreductases; C076865:vanillyl-alcohol oxidase