Open AccessCrystallization and preliminary X‐ray analysis of an alditol oxidase from Streptomyces coelicolor A3(2)
Author(s) -
Forneris Federico,
Rovida Stefano,
Heuts Dominic P. H. M.,
Fraaije Marco W.,
Mattevi Andrea
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106051128
Subject(s) - streptomyces coelicolor , crystallization , oxidase test , chemistry , cofactor , alcohol oxidoreductase , enzyme , crystallography , stereochemistry , organic chemistry , biochemistry , nad+ kinase , mutant , gene
Alditol oxidase is a 45 kDa enzyme containing a covalently bound FAD cofactor. This oxidase efficiently oxidizes a range of alditols to the corresponding aldoses. Owing to its substrate range and regioselectivity, this enzyme is an interesting candidate for biotechnological applications. Crystals of alditol oxidase from Streptomyces coelicolor A3(2) were obtained by the hanging‐drop vapour‐diffusion method and diffracted to 1.1 Å resolution. The crystals belong to space group C 2, with unit‐cell parameters a = 107, b = 68, c = 58 Å, β = 94°. Crystals of seleno‐ l ‐methionine‐labelled alditol oxidase were obtained after seeding the crystallization drops with native microcrystals and showed a diffraction limit of 2.4 Å.