title: Crystallization and preliminary X-ray diffraction analysis of pyranose 2-oxidase from the white-rot fungus Trametes multicolor.
abstract: Pyranose 2-oxidase (P2Ox) is a 270 kDa homotetrameric flavoenzyme that catalyzes the oxidation of D-glucose to 2-keto-D-glucose. P2Ox participates in lignin degradation by white-rot fungi and a tentative role of the enzyme is the production of H(2)O(2) for lignin peroxidases. Crystals of Trametes multicolor P2Ox were grown from monomethylether PEG 2000, sodium acetate, MgCl(2) and Ta(6)Br(12). They belong to space group P2(1), with unit-cell parameters a = 99.9, b = 101.7, c = 135.6 A, beta = 90.85 degrees. X-ray diffraction data to 2.0 A resolution were collected using synchrotron radiation. Self-rotation function calculations suggest that the asymmetric unit contains one homotetramer with 222 point-group symmetry.
authors.affiliation: Department of Biotechnology, KTH, Albanova University Center, SE-106 91 Stockholm, Sweden.
authors.forename: B Martin
authors.initials: BM
authors.lastname: Hallberg
authors.forename: Christian
authors.initials: C
authors.lastname: Leitner
authors.forename: Dietmar
authors.initials: D
authors.lastname: Haltrich
authors.forename: Christina
authors.initials: C
authors.lastname: Divne
mesh_terms: D001487:Basidiomycota / Q000201:enzymology*; D002237:Carbohydrate Dehydrogenases / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray
chemical_list: D002237:Carbohydrate Dehydrogenases; C022489:pyranose oxidase