Crystals of GlpE, a 12 kDa sulfurtransferase from Escherichia coli, display 1.06 Å resolution diffraction: A preliminary report

D. Bordo, T. J. Larson, J. L. Donahue, A. Spallarossa, M. Bolognesi

Research output: Contribution to journalArticle

Abstract

The Escherichia coli sn-glycerol 3-phosphate regulon contains the glpE gene coding for a 12 kDa protein which displays a sequence and a thiosulfate:cyanide sulfurtransferase activity similar to those of rhodanese enzymes. The GlpE protein was overexpressed, purified to homogeneity and crystallized in the trigonal space group P31 (or P32). The unit-cell parameters are a = b = 53.87, c = 30.52 Å, γ = 120°. Evaluation of the crystal packing parameter establishes the presence of one molecule per asymmetric unit, with a solvent content of 42%. The GlpE crystals display very high resolution diffraction; a 1.06 data set was collected using synchrotron radiation (λ = 0.9102 Å) with an overall completeness of 99.6%.

Original languageEnglish
Pages (from-to)1691-1693
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume56
Issue number12
DOIs
Publication statusPublished - 2000

ASJC Scopus subject areas

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

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