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EC Number
Crystallization
Reference
3.1 A resolution crystal structure of the Met142/Leu144 mutant
computational model of binding of inhibitor N-[4-[(6-aminopyridin-3-yl)amino]-3-methylbenzyl]-4-(trifluoromethyl)benzamide in the active site
crystals grow in space group P4(1)2(1)2 from polyethylene glycol using the hanging-drop method
hanging drop vapor diffusion method
hanging drop vapor diffusion method, crystal structure of IspDF, a bifunctional methylerythritol 4-phosphate cytidyltransferase methylerythritol 2,4-cyclodidiphosphate synthase
hanging-drop vapour diffusion method, X-ray crystal structures refined to 2.8 A resolution. The first structure contains a bound Mn2+ cation and the second structure contains CMP, 2-C-methyl-D-erythritol-2,4-cyclodiphosphate, and Mn2+
high-resolution structure, 16 A, of the enzyme in absence of substrate in the active site. Optimized crystals are obtained at a protein concentration of 35 mg/ml in a solution containing 4 M sodium formate and 5% glycerol. The crystals grow to avarage dimensions of 0.4 * 0.3 * 0.3 mM within a week
in complex with cytidine 5-monophosphate, at 2.3 A resolution. In contrast to bacterial enzymes, the cavity of Arabidopsis thaliana structure is unsuited for binding a diphosphate moiety
IspF-CDP complex, to 1.8 A resolution. IspF in complex with compound 6b, to 3.1 A resolution, belongs to space group I213 with unit cell parameter a = 144 A. IspF in complex with compound 7, to 2.7 A resolution, belongs to space group I213 with unit cell parameter a = 144.5 A. IspF in complex with cytosine arabinoside monophosphate, to 2.1 A resolution, belongs to space group P21 with unit cell parameters a = 88.8 A, b = 54.2 A, c = 118.4 A, beta = 95°. IspF in complex with 5-fluorocytidine, to 2.5 A resolution, belongs to space group C2 with unit cell parameters a = 104.68 A, b = 54.83 A, c = 88.51 A, beta = 99.66°. IspF in complex with cidofovir, to 2.8 A resolution, belongs to space group I213 with unit cell parameter a = 145.68 A
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