Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

Crystallization and preliminary X‐ray crystallographic analysis of dihydrouridine synthase from Thermus thermophilus and its complex with tRNA

Crystallization and preliminary X‐ray crystallographic analysis of dihydrouridine synthase from... Dihydrouridine synthase (Dus) is responsible for catalyzing dihydrouridine formation in RNA by the reduction of uridine. To elucidate its RNA‐recognition mechanism, Dus from Thermus thermophilus (TthDus) and its complex with tRNA were crystallized. Diffraction data sets were collected from crystals of native and selenomethionine‐substituted TthDus to resolutions of 1.70 and 2.30 Å, respectively. These crystals belonged to space group P1. Preliminary X‐ray crystallographic analysis showed that two molecules of TthDus were contained in an asymmetric unit. In addition, diffraction data were collected to 3.51 Å resolution from a crystal of selenomethionine‐substituted TthDus in complex with tRNA, which belonged to space group P41212. Preliminary structural analysis showed that the asymmetric unit contained two TthDus–tRNA complexes. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Crystallization and preliminary X‐ray crystallographic analysis of dihydrouridine synthase from Thermus thermophilus and its complex with tRNA

Loading next page...
 
/lp/wiley/crystallization-and-preliminary-x-ray-crystallographic-analysis-of-k8in4rY6h3

References (18)

Publisher
Wiley
Copyright
International Union of Crystallography, 2011
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S1744309111012486
pmid
21636912
Publisher site
See Article on Publisher Site

Abstract

Dihydrouridine synthase (Dus) is responsible for catalyzing dihydrouridine formation in RNA by the reduction of uridine. To elucidate its RNA‐recognition mechanism, Dus from Thermus thermophilus (TthDus) and its complex with tRNA were crystallized. Diffraction data sets were collected from crystals of native and selenomethionine‐substituted TthDus to resolutions of 1.70 and 2.30 Å, respectively. These crystals belonged to space group P1. Preliminary X‐ray crystallographic analysis showed that two molecules of TthDus were contained in an asymmetric unit. In addition, diffraction data were collected to 3.51 Å resolution from a crystal of selenomethionine‐substituted TthDus in complex with tRNA, which belonged to space group P41212. Preliminary structural analysis showed that the asymmetric unit contained two TthDus–tRNA complexes.

Journal

Acta Crystallographica Section FWiley

Published: Jun 1, 2011

There are no references for this article.