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Crystallization and preliminary X-ray data analysis of beta-alanine synthase from Drosophila melanogaster

  • Stina Lundgren
  • Birgit Andersen
  • Jure Piskur (Professor)
  • Doreen Dobritzsch
Publiceringsår: 2007
Språk: Engelska
Sidor: 874-877
Publikation/Tidskrift/Serie: Acta Crystallographica Section F Structural Biology and Crystallization Communications
Volym: 63
Dokumenttyp: Artikel
Förlag: Blackwell Publishing Ltd


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 angstrom at a synchrotron-radiation source, belong to space group C2 (unit-cell parameters a = 278.9, b = 95.0, c = 199.3 angstrom, beta = 125.8 degrees) and contain 8-10 molecules per asymmetric unit.



  • Biology and Life Sciences


  • ISSN: 1744-3091

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