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

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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. © 2012 International Union of Crystallography All rights reserved.

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Griffiths, S., Byrne, R. T., Antson, A. A., & Whelan, F. (2012). Crystallization and preliminary X-ray crystallographic analysis of the catalytic domain of human dihydrouridine synthase. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 68(3), 333–336. https://doi.org/10.1107/S1744309112003831

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