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crystals of the enzyme are grown at 18°C by the vapor-diffusion, hanging-drop method by mixing equal volumes of protein (4 mg/ml) and reservoir solution (100 mM Hepes (pH 7.0), 15% (w/v) PEG 1500, 100 mM NaCl (and 5 mM DTT in the case of the Se-Met protein)). Crystals grow within a few days as thin plates (0.15 mM x 0.15 mM x 0.050 mM) and belong to the orthorhombic space group P2(1)2(1)2(1) (a = 78 A, b = 88 A, c = 89 A) with two molecules in the asymmetric unit. Determination of the structure of the enzyme alone at 1.9 A resolution, and in complex with either ADP or the non-cleavable analog adenosine 5'-diphospho-2-deoxy-2-fluoro-L-glycero-beta-D-gluco-heptopyranoside (ADP-2-deoxy-2-fluoro-heptose) of the sugar donor at 2.4 A resolution. Both binary complexes offer a close view of the donor subsite and, together with results from site-directed mutagenesis studies, provide evidence for a model of the catalytic mechanism
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