5.3.3.2	hanging drop vapour diffusion method, selenomethionyl form, crystals display trigonal symmetry, with unit-cell parameters, a = b = 71.3 A, c = 61.7 A, and diffract to 1.45 A resolution	649155	
5.3.3.2	crystal structure of free and metal-bound C67A mutant enzyme	650979	
5.3.3.2	crystal structure of the isomerase-bromohydrin complex	651594	
5.3.3.2	hanging drop vapor diffusion method, crystal structures of complexes with transition state analogue N,N-dimethyl-2-amino-1-ethyl diphosphate and the covalently attached irreversible inhibitors 3,4-epoxy-3-methyl-1-butyl diphosphate at 1.96 A resolution	652367	
5.3.3.2	sitting drop vapor diffusion method, ligand-free form of the FMN-bound enzyme form at 2.8 A resolution. The octamer forms a D4 symmetrical open, cage-like structure. The monomers of 45000 Da display a classical TIM barrel fold	652916	
5.3.3.2	hanging drop vapor diffusion method, crystal structure of the C67A mutant of isopentenyl diphosphate isomerase complexed with the mechanism-based irreversible inhibitor 3,4-epoxy-3-methyl-1-butyl diphosphate	653840	
5.3.3.2	-	660922	
5.3.3.2	crystallographic investigation of phosphoantigen binding	661948	
5.3.3.2	crystals soaked with transition state analogue (N,N-dimethylamino)-1-ethyl diphosphate	680346	
5.3.3.2	of wild-type and mutants Y104A, Y104F	680660	
5.3.3.2	enzyme shows a flexible N-terminal alpha-helix covering the active pocket and blocking the entrance. Substrate binding induces conformational change in the active site. A water molecule is the direct proton donor for the substrate	681412	
5.3.3.2	native enzyme at 1.7 A and in complex with substrate at 1.9 A resolution. comparison with Escherichia coli enzyme structure	681413	
5.3.3.2	comparison of orthorhombic, monoclinic and trigonal crystal forms, up to 2.2 A resolution. Crystallization of free enzyme and in complex wih transition-state analogue N,N-dimethyl-2-amino-1-ethyl diphosphate	690288	
5.3.3.2	in complex with diphosphate. The diphosphate moiety is located near the conserved residues H10, R97, H152, Q157, E158, and W219, and the flavin cofactor. The putative active site may stabilize a carbocationic intermediate	690998	
5.3.3.2	molecular modeling of structure and comparison with structures of Streptococcus pneumoniae and Thermus thermophilus enzymes	695056	
5.3.3.2	the crystal structures of the substrate-free enzyme and of the substrate-enzyme complexes, in the oxidized and reduced states, are solved to resolutions between 1.99 and 3.1 A, six distinct types of type 2 IDI crystals are obtained	704638	
5.3.3.2	sitting drop vapor diffusion method, using 0.6 M calcium acetate and 50 mM HEPES pH 7.5	713655	
5.3.3.2	crystallized at 20°C using the hanging-drop vapor diffusion method with a reservoir solution containing 0.1 M Tris-HCl (pH 8.0), 0.2 M sodium citrate, and 30% (vol/vol) polyethylene glycol 400 (PEG 400)	719740	
5.3.3.2	the covalent adduct formed between irreversible mechanism based inhibitors, 3-methylene-4-penten-1-yl diphosphate or 3-oxiranyl-3-buten-1-yl diphosphate, and the flavin cofactor are investigated by X-ray crystallography and UV-visible spectroscopy. Both the crystal structures of enzyme binding the flavin-inhibitor adduct and the UV-visible spectra of the adducts indicate that the covalent bond is formed at C4a of flavin rather than at N5. The high-resolution crystal structures of enzyme-substrate complexes and the kinetic studies of new mutants confirm that only the flavin cofactor can catalyze protonation of the substrates and suggest that N5 of flavin is most likely to be involved in proton transfer	728667	
5.3.3.2	sitting drop vapor diffusion method, using HEPES buffer (100 mM, pH 7.5 with 2 M (NH4)2SO4)	747530