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

2 Citations (Scopus)

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

Fingerprint

Thiosulfate Sulfurtransferase
Escherichia
Escherichia coli
Diffraction
Display devices
proteins
Regulon
Crystals
Synchrotrons
cyanides
completeness
glycerols
Synchrotron radiation
diffraction
genes
crystals
homogeneity
enzymes
phosphates
synchrotron radiation

ASJC Scopus subject areas

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

Cite this

Crystals of GlpE, a 12 kDa sulfurtransferase from Escherichia coli, display 1.06 Å resolution diffraction : A preliminary report. / Bordo, D.; Larson, T. J.; Donahue, J. L.; Spallarossa, A.; Bolognesi, M.

In: Acta Crystallographica Section D: Biological Crystallography, Vol. 56, No. 12, 2000, p. 1691-1693.

Research output: Contribution to journalArticle

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