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 language | English |
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Pages (from-to) | 1691-1693 |
Number of pages | 3 |
Journal | Acta Crystallographica Section D: Biological Crystallography |
Volume | 56 |
Issue number | 12 |
DOIs | |
Publication status | Published - 2000 |
ASJC Scopus subject areas
- Clinical Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biophysics
- Condensed Matter Physics
- Structural Biology