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Crystallization and preliminary X-ray analysis of a bifunctional catalase-phenol oxidase from Scytalidium thermophilum

DOI: 10.1107/S1744309109012007 DOI Help
PMID: 19407383 PMID Help

Authors: Arwen R. Pearson (University of Leeds) , Simon E. V. Phillips (Diamond Light Source) , Michael J. Mcpherson (University of Leeds) , Didem Sutay Kocabas (Middle East Technical University) , Ufuk Bakir (Middle East Technical University) , Zumrut B. Ogel (Middle East Technical University) , Chi H. Trinh (University of Leeds)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology And Crystallization Communications , VOL 65 , PAGES 486-488

State: Published (Approved)
Published: May 2009
Diamond Proposal Number(s): 302

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 Å resolution at the Daresbury Synchrotron Radiation Source. The crystals belonged to space group P21 and contained one tetramer per asymmetric unit.

Subject Areas: Biology and Bio-materials


Instruments: I02-Macromolecular Crystallography , I03-Macromolecular Crystallography , I04-Macromolecular Crystallography