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Crystallization and preliminary X-ray crystallographic analysis of the catalytic domain of human dihydrouridine synthase
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| Journal | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
|---|---|
| Date | E-pub ahead of print - 22 Feb 2012 |
| Date | Published (current) - 2012 |
| Issue number | Pt 3 |
| Volume | 68 |
| Number of pages | 4 |
| Pages (from-to) | 333-336 |
| Early online date | 22/02/12 |
| Original language | English |
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.
Bibliographical note
© 2012 International Union of Crystallography
- Catalytic Domain, Crystallization, Crystallography, X-Ray, Humans, Oxidoreductases
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