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Purification, crystallization and X-ray diffraction analysis of dihydropyrimidinase from Dictyostelium discoideum
Karolinska Institutet. (Molecular Structural Biology)
2006 (English)In: Acta Crystallographica. Section F: Structural Biology and Crystallization Communications, ISSN 1744-3091, E-ISSN 1744-3091, Vol. 62, no Pt 1, 36-38 p.Article in journal (Refereed) Published
Abstract [en]

Dihydropyrimidinase (EC 3.5.2.2) is the second enzyme in the reductive pyrimidine-degradation pathway and catalyses the hydrolysis of 5,6-dihydrouracil and 5,6-dihydrothymine to the corresponding N-carbamylated beta-amino acids. The recombinant enzyme from the slime mould Dictyostelium discoideum was overexpressed, purified and crystallized by the vapour-diffusion method. One crystal diffracted to better than 1.8 A resolution on a synchrotron source and was shown to belong to space group I222, with unit-cell parameters a = 84.6, b = 89.6, c = 134.9 A and one molecule in the asymmetric unit.

Place, publisher, year, edition, pages
2006. Vol. 62, no Pt 1, 36-38 p.
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Structural Biology
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URN: urn:nbn:se:uu:diva-214435DOI: 10.1107/S174430910503976XISI: 000234169100011PubMedID: 16511257OAI: oai:DiVA.org:uu-214435DiVA: diva2:684947
Available from: 2014-01-08 Created: 2014-01-08 Last updated: 2017-12-06Bibliographically approved

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Dobritzsch, Doreen

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