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

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Publication details

JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
DateE-pub ahead of print - 22 Feb 2012
DatePublished (current) - 2012
Issue numberPt 3
Number of pages4
Pages (from-to)333-336
Early online date22/02/12
Original languageEnglish


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.

Bibliographical note

© 2012 International Union of Crystallography

    Research areas

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

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