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Crystallization and preliminary X-ray analysis of beta-alanine synthase from the yeast Saccharomyces kluyveri
Karolinska Institutet. (Molecular Structural Biology)
2003 (English)In: Acta Crystallographica Section D: Biological Crystallography, ISSN 0907-4449, E-ISSN 1399-0047, Vol. 59, no Pt 7, 1267-1269 p.Article in journal (Refereed) Published
Abstract [en]

In eukaryotes and some bacteria, the third step of reductive pyrimidine catabolism is catalyzed by beta-alanine synthase (EC 3.5.1.6). Crystals of the recombinant enzyme from the yeast Saccharomyces kluyveri were obtained using sodium citrate as a precipitant. The crystals belong to space group P2(1) (unit-cell parameters a = 117.2, b = 77.1, c = 225.5 A, beta = 95.0 degrees ) and contain four homodimers per asymmetric unit. Data were collected to 2.7 A resolution. Introduction of heavy atoms into the crystal lattice induced a different set of unit-cell parameters (a = 61.0, b = 77.9, c = 110.1 A, beta = 97.2 degrees ) in the same space group P2(1), with only one homodimer per asymmetric unit.

Place, publisher, year, edition, pages
2003. Vol. 59, no Pt 7, 1267-1269 p.
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Structural Biology
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URN: urn:nbn:se:uu:diva-214441DOI: 10.1107/S0907444903009120ISI: 000183809900029PubMedID: 12832781OAI: oai:DiVA.org:uu-214441DiVA: diva2:684934
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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