FB2026_03 , released September 17, 2026
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Citation
Lundgren, S., Andersen, B., Piskur, J., Dobritzsch, D. (2007). Crystallization and preliminary X-ray data analysis of beta-alanine synthase from Drosophila melanogaster.  Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63(Part 10): 874--877.
FlyBase ID
FBrf0201709
Publication Type
Research paper
Abstract
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.
PubMed ID
PubMed Central ID
PMC2339735 (PMC) (EuropePMC)
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    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Journal
    Abbreviation
    Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
    Title
    Acta crystallographica. Section F, Structural biology and crystallization communications
    ISBN/ISSN
    1744-3091
    Data From Reference
    Genes (1)