PMID:14993681
| Citation |
Giabbai, B and Degano, M (2004) Cloning, purification, crystallization and X-ray analysis of the Escherichia coli pyrimidine nucleoside hydrolase YeiK. Acta Crystallogr. D Biol. Crystallogr. 60:524-7 |
|---|---|
| Abstract |
The E. coli yeiK gene product is homologous to members of the nucleoside hydrolase family of enzymes, the physiological role of which in bacteria is still unknown. Here, the cloning, expression in milligram quantities and enzymatic characterization of YeiK as a pyrimidine-specific nucleoside hydrolase is reported. Crystals of YeiK diffract X-rays to a resolution of 1.7 A and belong to the triclinic crystal system in space group P1, with unit-cell parameters a = 44.81, b = 85.71, c = 90.68 A, alpha = 112.95, beta = 101.95, gamma = 85.92 degrees. |
| Links |
PubMed Online version:10.1107/S0907444903028488 |
| Keywords |
Cloning, Molecular; Crystallization; Crystallography, X-Ray; Escherichia coli/enzymology; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/isolation & purification; Gene Expression; N-Glycosyl Hydrolases/chemistry; N-Glycosyl Hydrolases/isolation & purification; Recombinant Fusion Proteins/chemistry; Recombinant Fusion Proteins/isolation & purification |
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