Crystals of GlpE, a 12 kDa sulfurtransferase from escherichia coli, display 1.06 A 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 thiosulfatecyanide sulfurtransferase activity similar to those of rhodanese enzymes. The GlpE protein was overexpressed, purified to homogeneity and crystallized in the trigonal space group P3(1) (or P3(2)). The unit-cell parameters are a = b = 53.87, c = 30.52 A, gamma = 120 degrees. 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 (lambda = 0.9102 A) with an overall completeness of 99.6%.