Crystallization and preliminary X-ray analysis of beta-alanine synthase from the yeast Saccharomyces kluyveri

D. Dobritzsch, Zoran Gojkovic, Birgit Andersen, Jure Piskur

    Research output: Contribution to journalJournal articleResearchpeer-review

    Abstract

    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 Angstrom, beta=95.0degrees) and contain four homodimers per asymmetric unit. Data were collected to 2.7 Angstrom 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 Angstrom, beta=97.2degrees) in the same space group P2(1), with only one homodimer per asymmetric unit.
    Original languageEnglish
    JournalActa Crystallographica Section D-Biological Crystallography
    Volume59
    Pages (from-to)1267-1269
    ISSN0907-4449
    DOIs
    Publication statusPublished - 2003

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