Crystallization and preliminary crystallographic analysis of the central domain of Drosophila Dribble, a protein that is essential for ribosome biogenesis

A soluble domain spanning amino-acid residues 16–197 of the Drosophila Dribble protein was overexpressed in E. coli, purified and crystallized. X-ray diffraction data were collected to beyond 2 Å resolution. 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 P2₁2₁2₁. Data were collected that extended to beyond 2 Å resolution