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Crystallization and preliminary X-ray data analysis of beta-alanine synthase from Drosophila melanogaster
Karolinska Institutet. (Molecular Structural Biology)
2007 (English)In: Acta Crystallographica. Section F: Structural Biology and Crystallization Communications, ISSN 1744-3091, E-ISSN 1744-3091, Vol. 63, no Pt 10, 874-877 p.Article in journal (Refereed) Published
Abstract [en]

Beta-alanine synthase catalyzes the last step in the reductive degradation pathway for uracil and thymine, which represents the main clearance route for the widely used anticancer drug 5-fluorouracil. Crystals of the recombinant enzyme from Drosophila melanogaster, which is closely related to the human enzyme, were obtained by the hanging-drop vapour-diffusion method. They diffracted to 3.3 A at a synchrotron-radiation source, belong to space group C2 (unit-cell parameters a = 278.9, b = 95.0, c = 199.3 A, beta = 125.8 degrees) and contain 8-10 molecules per asymmetric unit.

Place, publisher, year, edition, pages
2007. Vol. 63, no Pt 10, 874-877 p.
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Structural Biology
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URN: urn:nbn:se:uu:diva-214430DOI: 10.1107/S1744309107042984ISI: 000250012400014PubMedID: 17909293OAI: oai:DiVA.org:uu-214430DiVA: diva2:684954
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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