EC Number   |
|---|
    2.5.1.78 | - |
| 2.5.1.78 | at 3.57 A resolution. Crystals belong to monoclinic space group P21, with 60 subunits per asymmetric unit, packed as an icosahedron. Enzyme contains an N-terminal proline residue |
| 2.5.1.78 | crystal structure analysis of reconstituted, icosahedral beta-subunit capsids with bound substrate analogue inhibitor (5-nitro-6-(D-ribitylamino)-2,4(1H,3H)-pyrimidinedione) at 2.4 A resolution |
| 2.5.1.78 | crystallized at room temperature by sitting-drop vapor-diffusion method, the protein is crystallized in the cubic space group I23 with the cell dimensions a = b = c = 180.8 A, diffraction data are collected to 1.6 A resolution |
| 2.5.1.78 | crystallized in sitting drops by vapor diffusion. The crystal structure of lumazine synthase from Candida albicans is solved by molecular replacement and refined at 2.5 A resolution. The results of crystallographic investigations and sedimentation equilibrium experiments clearly indicate the presence of pentameric assemblies of the enzyme either in crystals or in solution |
| 2.5.1.78 | crystallized in the presence of two inhibitor compounds 3-(1,3,7-trihydro-9-D-ribityl-2,6,8-purinetrione-7-yl)propane 1-phosphate and 3-(1,3,7-trihydro-9-D-ribityl-2,6,8-purinetrion-7-yl)butane 1-phosphate. The crystals are obtained in sitting drops by the vapor diffusion technique with the following macroseeding procedure |
| 2.5.1.78 | crystals are grown at 18°C by the sitting drop vapor diffusion method. The W27Y mutant protein in complex with riboflavin, the substrate analogue 5-nitroso-6-ribitylamino-2,4(1H,3H)-pyrimidinedione, and the product analogue 6-carboxyethyl-7-oxo-8-ribityllumazine, are determined by X-ray crystallography at resolutions of 2.72.8 A |
| 2.5.1.78 | crystals are obtained by means of the hanging-drop, vapor-diffusion method at room temperature |
| 2.5.1.78 | crystals are obtained in sitting drops by the vapour diffusion technique with the macroseeding procedure |
| 2.5.1.78 | in complex with inhibitor N-6-(ribitylamino)pyrimidine-2,4(1H,3H)-dion-5-ylpropionamide and phosphate, to 2.3 A resolution. The aromatic ring of the inhibitor is packed in the hydrophobic environment in the active site formed by Trp27, Ile60, Val81 and Val82, Ile83, Phe90, and Val93 residues of one subunit. The pyrimidine ring is in stacking interaction with the indole ring of Trp27 at a distance of 4 A |
