Crystallization and preliminary crystallographic analysis of the central domain of Drosophila Dribble, a protein that is essential for ribosome biogenesis.
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.
Cheng
Tat Cheung
TC
Department of Biochemistry, The Chinese University of Hong Kong, Shatin New Town, Hong Kong, People's Republic of China.
Chen
Yu Wai
YW
Wong
Kam Bo
KB
Ngai
Sai-Ming
SM
Chan
H Y Edwin
HY
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
D029721:Drosophila Proteins; D009687:Nuclear Proteins; C434386:dbe protein, Drosophila
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