Cloning, purification, crystallization and X-ray analysis of the Escherichia coli pyrimidine nucleoside hydrolase YeiK

Barbara Giabbai, Massimo Degano

Research output: Contribution to journalArticle

4 Citations (Scopus)

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 Å and belong to the triclinic crystal system in space group P1, with unit-cell parameters a = 44.81, b = 85.71, c = 90.68 Å, α = 112.95, β = 101.95, γ= 85.92°.

Original languageEnglish
Pages (from-to)524-527
Number of pages4
JournalActa Crystallographica Section D: Biological Crystallography
Volume60
Issue number3
DOIs
Publication statusPublished - Mar 2004

Fingerprint

N-Glycosyl Hydrolases
Pyrimidine Nucleosides
nucleosides
Cloning
X ray analysis
pyrimidines
Escherichia
Crystallization
purification
Escherichia coli
Purification
Organism Cloning
X-Rays
crystallization
Crystals
genes
bacteria
crystals
enzymes
Bacteria

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics
  • Clinical Biochemistry
  • Structural Biology
  • Condensed Matter Physics

Cite this

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