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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 (DBE16-197) was produced for structural determination. In this report, the crystallization and preliminary X-­ray diffraction data analysis of the DBE16-197 protein domain are described. Crystals of DBE16-197 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.

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