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Purification, crystallization and X-ray diffraction analysis of dihydropyrimidinase from Dictyostelium discoideum

  • B Lohkamp
  • Birgit Andersen
  • Jure Piskur
  • D Dobritzsch
Publiceringsår: 2006
Språk: Engelska
Sidor: 36-38
Publikation/Tidskrift/Serie: Acta Crystallographica. Section F: Structural Biology and Crystallization Communications2005-01-01+01:002014-01-01+01:00
Volym: 62
Nummer: 1
Dokumenttyp: Artikel i tidskrift
Förlag: Wiley-Blackwell


Dihydropyrimidinase (EC is the second enzyme in the reductive pyrimidine-degradation pathway and catalyses the hydrolysis of 5,6-dihydrouracil and 5,6-dihydrothymine to the corresponding N-carbamylated beta-amino acids. The recombinant enzyme from the slime mould Dictyostelium discoideum was overexpressed, purified and crystallized by the vapour-diffusion method. One crystal diffracted to better than 1.8 angstrom resolution on a synchrotron source and was shown to belong to space group I222, with unit-cell parameters a = 84.6, b = 89.6, c = 134.9 angstrom and one molecule in the asymmetric unit.


  • Biological Sciences


  • ISSN: 2053-230X

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