Open AccessCrystallization and preliminary X‐ray crystallographic analysis of the catalytic domain of human dihydrouridine synthase
Author(s) -
Griffiths Sam,
Byrne Robert T.,
Antson Alfred A.,
Whelan Fiona
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112003831
Subject(s) - atp synthase , crystallization , crystallography , resolution (logic) , biology , chemistry , enzyme , biochemistry , organic chemistry , artificial intelligence , computer science
Dihydrouridine synthases catalyse the reduction of uridine to dihydrouridine in the D‐loop and variable loop of tRNA. The human dihydrouridine synthase Hs Dus2L has been implicated in the development of pulmonary carcinogenesis. Here, the purification, crystallization and preliminary X‐ray characterization of the Hs Dus2L catalytic domain are reported. The crystals belonged to space group P 2 1 and contained a single molecule of Hs Dus2L in the asymmetric unit. A complete data set was collected to 1.9 Å resolution using synchrotron radiation.