Search: onr:"swepub:oai:DiVA.org:kth-23033" >
Crystallization and...
Crystallization and preliminary X-ray diffraction analysis of pyranose 2-oxidase from the white-rot fungus Trametes multicolor
-
- Hällberg, B. Martin (author)
- KTH,Bioteknologi
-
- Leitner, Christian (author)
- KTH,Bioteknologi
-
- Haltrich, Dietmar (author)
- KTH,Bioteknologi
-
show more...
-
- Divne, Christina (author)
- KTH,Bioteknologi
-
show less...
-
(creator_code:org_t)
- 2003-12-18
- 2004
- English.
-
In: Acta Crystallographica Section D. - : International Union of Crystallography (IUCr). - 0907-4449 .- 1399-0047. ; 60, s. 197-199
- Related links:
-
https://urn.kb.se/re...
-
show more...
-
https://doi.org/10.1...
-
show less...
Abstract
Subject headings
Close
- 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 H2O2 for lignin peroxidases. Crystals of Trametes multicolor P2Ox were grown from monomethylether PEG 2000, sodium acetate, MgCl2 and Ta6Br12. They belong to space group P2(1), with unit-cell parameters a = 99.9, b = 101.7, c = 135.6 Angstrom, beta = 90.85degrees. X-ray diffraction data to 2.0 Angstrom resolution were collected using synchrotron radiation. Self-rotation function calculations suggest that the asymmetric unit contains one homotetramer with 222 point-group symmetry.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Keyword
- phanerochaete-chrysosporium
- rotation function
- crystal-structure
- screening method
- oxidase
- proteins
- versicolor
- cultures
- program
Publication and Content Type
- ref (subject category)
- art (subject category)
Find in a library
To the university's database