EC Number   |
|---|
    1.1.3.15 | 3.0 A resolution, octamer with non-crystallographic two- and four-fold axes |
| 1.1.3.15 | ammonium sulfate precipitation, 2.6 A resolution of a two subunit apoenzyme |
| 1.1.3.15 | analysis of the crystal structure of enzyme LCHAO in complex with cofactor FMN and inhibitor 4-carboxy-5-[(4-chlorophenyl)sulfanyl]-1,2,3-thiadiazole (CCPST) at 1.3 A resolution |
| 1.1.3.15 | apo-GOX structure and its complex structure with cofactor FMN. The binding of FMN induces a pronounced conformational change of the GOX tetramer. A conserved pH sensor found among different species might directly regulate the binding of FMN and the enzyme activity |
| 1.1.3.15 | hanging-drop or sitting-drop vapour diffusion method, 2.44 A resolution, large diffracting crystals of LOXR181M are obtained. LOX-R181M crystals belong to the tetragonal space group I422, with unit-cell parameters a = b = 192.632 A, c= 200.263 A, alpha = beta = gamma =90°. There are four monomers in the asymmetric unit |
| 1.1.3.15 | resolution to 1.9 A. One pyruvate molecule is bound to the active site and located near N5 position of FMN for subunits, A, B, and D in the asymmetric unit. The pyruvate molecule is stabilized by the interaction of its carboxylate group with the side-chain atoms of Tyr40, Arg181, His265, and Arg268, and of its keto-oxygen atom with the side-chain atoms of Tyr146, Tyr215, and His265 |
| 1.1.3.15 | sitting drop vapor diffusion method, 0.005 ml of protein solution containing 10 mg/ml protein in 0.1 M Tris, pH 7.5, mixed with the same volume of reservoir solution containing 0.4 M sodium acetate and 0.2 M sodium citrate, pH 6.5, equilibration at 4°C, soaking of crystals in 25% glycerol-containing reservoir solution, X-ray diffraction structure determination and analysis at 2.3 A resolution |
| 1.1.3.15 | sitting-drop vapor diffusion technique. Crystal structure of wild-type enzyme at 2.1 A resolution. Space group I422 of unit-cell parameters a = b = 191.096 A, c = 194.497 A and alpha = beta = gamma = 90° with four monomers per asymmetric unit |
| 1.1.3.15 | sitting-drop vapour-diffusion method, determination of structure at 2.1 A resolution |
| 1.1.3.15 | structures of recombinant GO complexed with sulfate, glyoxylate, and 4-carboxy-5-dodecylsulfanyl-1,2,3-triazole (CDST), determined by X-ray crystallography are reported. A loop region (loop 4), is completely visible when the GO active site contains a small ligand. Lack of electron density for this loop in the GOCDST complex, mimicking a large substrate, indicates that a disordered to ordered transition occurs with substrate binding. Conformational flexibility of Trp110 is responsible for enabling GO to react with R-hydroxy acids. Movement of Trp110 disrupts a hydrogen-bonding network between Trp110, Leu191, Tyr134, and Tyr208. This loss indicates that active site movements are directly linked to changes in the conformation of loop 4 |
