title: Crystallization and preliminary X-ray crystallographic analysis of the catalytic domain of human dihydrouridine synthase.
abstract: 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.
authors.affiliation: York Structural Biology Laboratory, Department of Chemistry, The University of York, Heslington, England.
authors.forename: Sam
authors.initials: S
authors.lastname: Griffiths
authors.forename: Robert T
authors.initials: RT
authors.lastname: Byrne
authors.forename: Alfred A
authors.initials: AA
authors.lastname: Antson
authors.forename: Fiona
authors.initials: F
authors.lastname: Whelan
mesh_terms: D020134:Catalytic Domain; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D010088:Oxidoreductases / Q000032:analysis / Q000737:chemistry*
chemical_list: D010088:Oxidoreductases; C526987:tRNA dihydrouridine synthase-2, human