Acta Cryst. (2006). F62, 930-934 [ doi:10.1107/S1744309106030107 ]
Abstract: The cloning, expression, purification, crystallization and preliminary crystallographic analysis of glucose-1-phosphate uridylyltransferase (UgpG) from Sphingomonas elodea ATCC 31461 bound to glucose-1-phosphate are reported. Diffraction data sets were obtained from seven crystal forms in five different space groups, with highest resolutions ranging from 4.20 to 2.65 Å. The phase problem was solved for a P21 crystal form using multiple isomorphous replacement with anomalous scattering from an osmium derivative and a SeMet derivative. The best native crystal in space group P21 has unit-cell parameters a = 105.5, b = 85.7, c = 151.8 Å,
= 105.2°. Model building and refinement are currently under way.
Keywords: GalU; UgpG; RmlA; pyrophosphorylase; sugar activation.
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