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 |
|---|---|
| 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 |
Fingerprint
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 journal › Article
}
TY - JOUR
T1 - Crystals of GlpE, a 12 kDa sulfurtransferase from Escherichia coli, display 1.06 Å resolution diffraction
T2 - A preliminary report
AU - Bordo, D.
AU - Larson, T. J.
AU - Donahue, J. L.
AU - Spallarossa, A.
AU - Bolognesi, M.
PY - 2000
Y1 - 2000
N2 - 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%.
AB - 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%.
UR - http://www.scopus.com/inward/record.url?scp=0034522515&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0034522515&partnerID=8YFLogxK
U2 - 10.1107/S0907444900015304
DO - 10.1107/S0907444900015304
M3 - Article
C2 - 11092948
AN - SCOPUS:0034522515
VL - 56
SP - 1691
EP - 1693
JO - Acta Crystallographica Section D: Biological Crystallography
JF - Acta Crystallographica Section D: Biological Crystallography
SN - 0907-4449
IS - 12
ER -