Crystallization and X-ray diffraction analysis of dihydropyrimidinase from Saccharomyces kluyveri
- Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm (Sweden)
- Department of Cell and Organism Biology, Lund University, Lund (Sweden)
Dihydropyrimidinase from the yeast S. kluyveri was crystallized by vapour diffusion. The crystals belong to space group P2{sub 1} (unit-cell parameters a = 91.0, b = 73.0, c = 161.4 Å, β = 91.4°) and diffracted to 2.6 Å resolution. Dihydropyrimidinase (EC 3.5.2.2) catalyzes the second step in the reductive pathway of pyrimidine degradation, the hydrolysis of 5,6-dihydrouracil and 5,6-dihydrothymine to the corresponding N-carbamylated β-amino acids. Crystals of the recombinant enzyme from the yeast Saccharomyces kluyveri diffracting to 2.6 Å at a synchrotron-radiation source have been obtained by the hanging-drop vapour-diffusion method. They belong to space group P2{sub 1} (unit-cell parameters a = 91.0, b = 73.0, c = 161.4 Å, β = 91.4°), with one homotetramer per asymmetric unit.
- OSTI ID:
- 22356110
- Journal Information:
- Acta Crystallographica. Section F, Vol. 61, Issue Pt 4; Other Information: PMCID: PMC1952421; PMID: 16511040; PUBLISHER-ID: en5103; OAI: oai:pubmedcentral.nih.gov:1952421; Copyright (c) International Union of Crystallography 2005; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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