Crystallization and preliminary X-ray crystallographic analysis of the catalytic domain of human dihydrouridine synthase

Sam Griffiths, Robert T Byrne, Alfred A Antson, Fiona Whelan

Research output: Contribution to journalArticlepeer-review


Dihydrouridine synthases catalyse the reduction of uridine to dihydrouridine in the D-loop and variable loop of tRNA. The human dihydrouridine synthase HsDus2L has been implicated in the development of pulmonary carcinogenesis. Here, the purification, crystallization and preliminary X-ray characterization of the HsDus2L catalytic domain are reported. The crystals belonged to space group P2(1) and contained a single molecule of HsDus2L in the asymmetric unit. A complete data set was collected to 1.9 Å resolution using synchrotron radiation.

Original languageEnglish
Pages (from-to)333-336
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Issue numberPt 3
Early online date22 Feb 2012
Publication statusPublished - 2012

Bibliographical note

© 2012 International Union of Crystallography


  • Catalytic Domain
  • Crystallization
  • Crystallography, X-Ray
  • Humans
  • Oxidoreductases

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