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

doi:10.1107/S0907444900015304

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

A.O.U. San Martino - IST, Istituto Nazionale Ricerca sul Cancro (GENOVA)

Research output: Contribution to journal › Article

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	https://doi.org/10.1107/S0907444900015304
Publication status	Published - 2000

ASJC Scopus subject areas

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

Access to Document

10.1107/S0907444900015304

Fingerprint Dive into the research topics of 'Crystals of GlpE, a 12 kDa sulfurtransferase from Escherichia coli, display 1.06 Å resolution diffraction: A preliminary report'. Together they form a unique fingerprint.

Cite this

Bordo, D., Larson, T. J., Donahue, J. L., Spallarossa, A., & Bolognesi, M. (2000). Crystals of GlpE, a 12 kDa sulfurtransferase from Escherichia coli, display 1.06 Å resolution diffraction: A preliminary report. Acta Crystallographica Section D: Biological Crystallography, 56(12), 1691-1693. https://doi.org/10.1107/S0907444900015304

@article{d414efa25411459d8ec43c96cd8f4400,

title = "Crystals of GlpE, a 12 kDa sulfurtransferase from Escherichia coli, display 1.06 {\AA} resolution diffraction: A preliminary report",

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 {\AA}, 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 {\AA}) with an overall completeness of 99.6%.",

author = "D. Bordo and Larson, {T. J.} and Donahue, {J. L.} and A. Spallarossa and M. Bolognesi",

year = "2000",

doi = "10.1107/S0907444900015304",

language = "English",

volume = "56",

pages = "1691--1693",

journal = "Acta Crystallographica Section D: Biological Crystallography",

issn = "0907-4449",

publisher = "International Union of Crystallography",

number = "12",

}

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 -