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

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Date

2009-05-01

Author

Kocabas, Didem Sutay
Pearson, Arwen R.
Phillips, Simon E. V.
Bakir, Ufuk
Ögel, Zümrüt Begüm
McPherson, Michael J.
Trinh, Chi H.

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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 angstrom resolution at the Daresbury Synchrotron Radiation Source. The crystals belonged to space group P2(1) and contained one tetramer per asymmetric unit.

Subject Keywords

Penicillium-vitale, Purification

URI

https://hdl.handle.net/11511/51550

Journal

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS

DOI

https://doi.org/10.1107/s1744309109012007

Collections

Graduate School of Natural and Applied Sciences, Article

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Citation Formats

D. S. Kocabas et al., “Crystallization and preliminary X-ray analysis of a bifunctional catalase-phenol oxidase from Scytalidium thermophilum,” ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS, pp. 486–488, 2009, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/51550.