Open AccessCrystallization and preliminary crystallographic analysis of the central domain of Drosophila Dribble, a protein that is essential for ribosome biogenesis
Author(s) -
Cheng TatCheung,
Chen Yu Wai,
Wong KamBo,
Chan H. Y. Edwin
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110011206
Subject(s) - crystallization , crystallography , biogenesis , ribosome biogenesis , domain (mathematical analysis) , ribosome , resolution (logic) , germ , chemistry , biology , biochemistry , microbiology and biotechnology , rna , gene , mathematical analysis , mathematics , organic chemistry , artificial intelligence , computer science
Dribble (DBE) is a Drosophila protein that is essential for ribosome biogenesis. Bioinformatics analysis revealed a folded central domain of DBE which is flanked by structural disorder in the N‐ and C‐terminal regions. The protein fragment spanning amino‐acid residues 16–197 (DBE 16–197 ) was produced for structural determination. In this report, the crystallization and preliminary X‐ray diffraction data analysis of the DBE 16–197 protein domain are described. Crystals of DBE 16–197 were grown by the sitting‐drop vapour‐diffusion method at 289 K using ammonium phosphate as a precipitant. The crystals belonged to space group P 2 1 2 1 2 1 . Data were collected that extended to beyond 2 Å resolution.