title: Crystallization and preliminary X-ray analysis of a bifunctional catalase-phenol oxidase from Scytalidium thermophilum.
abstract: Catalase-phenol oxidase from Scytalidium thermophilum is a bifunctional enzyme: its major activity is the catalase-mediated decomposition of hydrogen peroxide, but it also catalyzes phenol oxidation. To understand the structural basis of this dual functionality, the enzyme, which has been shown to be a tetramer in solution, has been purified by anion-exchange and gel-filtration chromatography and has been crystallized using the hanging-drop vapour-diffusion technique. Streak-seeding was used to obtain larger crystals suitable for X-ray analysis. Diffraction data were collected to 2.8 A resolution at the Daresbury Synchrotron Radiation Source. The crystals belonged to space group P2(1) and contained one tetramer per asymmetric unit.
authors.affiliation: Chemical Engineering Department, Middle East Technical University, Ankara, Turkey. didemsutay@gmail.com
authors.forename: Didem
authors.initials: D
authors.lastname: Sutay Kocabas
authors.forename: Arwen R
authors.initials: AR
authors.lastname: Pearson
authors.forename: Simon E V
authors.initials: SE
authors.lastname: Phillips
authors.forename: Ufuk
authors.initials: U
authors.lastname: Bakir
authors.forename: Zumrut B
authors.initials: ZB
authors.lastname: Ogel
authors.forename: Michael J
authors.initials: MJ
authors.lastname: McPherson
authors.forename: Chi H
authors.initials: CH
authors.lastname: Trinh
mesh_terms: D001203:Ascomycota / Q000201:enzymology* / Q000235:genetics; D002374:Catalase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D014442:Monophenol Monooxygenase / Q000032:analysis* / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: D002374:Catalase; D014442:Monophenol Monooxygenase