Crystallization and preliminary crystallographic analysis of galactose-1-phosphate uridylyltransferase from Escherichia coli.
Galactose-1-phosphate uridylyltransferase catalyzes the formation of UDP-galactose during normal cellular metabolism, making it an essential enzyme in all cells. The enzyme from Escherichia coli has been crystallized at pH 5.9 in the presence of phenyl-UDP (P(1)-5'-uridyl-P(2)-phenyl diphosphate), a substrate analog, using PEG 10 000 in combination with Li(2)SO(4) and NaCl. Crystals belong to space group P2(1)2(1)2 with unit-cell dimensions a = 58.6, b = 217.6 and c = 69.6 A. There is one dimer or two subunits in the asymmetric unit. Crystals are relatively insensitive to X-ray radiation and diffract beyond 2.5 A resolution. A low-resolution native data set has been recorded.
Institute for Enzyme Research, Graduate School, University of Wisconsin, Madison 53705, USA.
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Wedekind
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Frey
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Rayment