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 A, gamma = 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 A data set was collected using synchrotron radiation (wavelength = 0.9102 A) with an overall completeness of 99.6%.
Crystals of GlpE, a 12 kDa sulfurtransferase from Escherichia coli, display 1.06 Å resolution diffraction: a preliminary report
SPALLAROSSA, ANDREA;
2000-01-01
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 A, gamma = 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 A data set was collected using synchrotron radiation (wavelength = 0.9102 A) with an overall completeness of 99.6%.
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