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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.

SUBMITTER: Griffiths S

PROVIDER: S-EPMC3310545 | biostudies-literature | 2012 Mar

REPOSITORIES: biostudies-literature

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

Griffiths Sam S Byrne Robert T RT Antson Alfred A AA Whelan Fiona F

Acta crystallographica. Section F, Structural biology and crystallization communications 20120222 Pt 3

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 ...[more]

PMID: 22442237

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