title: Crystallization and preliminary crystallographic analysis of the central domain of Drosophila Dribble, a protein that is essential for ribosome biogenesis.
abstract: 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 P2(1)2(1)2(1). Data were collected that extended to beyond 2 A resolution.
authors.affiliation: Department of Biochemistry, The Chinese University of Hong Kong, Shatin New Town, Hong Kong, People's Republic of China.
authors.forename: Tat Cheung
authors.initials: TC
authors.lastname: Cheng
authors.forename: Yu Wai
authors.initials: YW
authors.lastname: Chen
authors.forename: Kam Bo
authors.initials: KB
authors.lastname: Wong
authors.forename: Sai-Ming
authors.initials: SM
authors.lastname: Ngai
authors.forename: H Y Edwin
authors.initials: HY
authors.lastname: Chan
mesh_terms: D000818:Animals; D018360:Crystallography, X-Ray; D029721:Drosophila Proteins / Q000737:chemistry* / Q000378:metabolism; D004331:Drosophila melanogaster / Q000737:chemistry*; D009687:Nuclear Proteins / Q000737:chemistry* / Q000378:metabolism; D012270:Ribosomes / Q000378:metabolism*; D013696:Temperature
chemical_list: D029721:Drosophila Proteins; D009687:Nuclear Proteins; C434386:dbe protein, Drosophila
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