Crystals of GlpE, a 12 kDa sulfurtransferase from Escherichia coli, display 1.06 Å resolution diffraction: a preliminary report

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 Å data set was collected using synchrotron radiation (λ = 0.9102 Å) with an overall completeness of 99.6%.