EC Number   |
|---|
   1.20.99.1 | free enzyme or enzyme complexed with arsenate and arsenite, X-ray diffraction structure determination and analysis at 1.65 A and 1.26 A, respecively |
| 1.20.99.1 | in complex with arsenitate and arsenite and enzyme alone. Native structure shows sulfate and sulfite ions binding in the active site as analogs of arsenate and arsenite. Arsenate forms a covlaent adduct with C12 in the active site, showing tetrahedral geometry. The corresponding adduct with arsenite binds as thiarsahydroxy adduct. High number of 385 water molecules bound to crystal structure |
| 1.20.99.1 | purified recombinant wild-type and SeMet-labeled enzyme, 4°C, PEG or PEG methyl ether is utilized as main precipitant, 2 crystal forms, X-ray diffraction structure determination and analysis at 2.2 A, flash-annealing technique |
| 1.20.99.1 | purified wild-type and selenomethionine-labeled enzyme, hanging drop vapour diffusion method, enzyme in 0.1 M sodium acetate, pH 4.4-4.6, 0.2 M ammonium sulfate, in presence of 30-35% PEG methyl ether, and 5 mM DTT, crystal structure in reduced form, X-ray diffraction structure determination and analysis at 1.6-2.4 A resolution |
| 1.20.99.1 | recombinant protein, space group P321 |
| 1.20.99.1 | solution structure and backbone dynamics of both the reduced and oxidized forms of enzyme. Reduced from undergoes millisecond conformational changes in the functional P-loop and C82-C89. In the oxidized form, C82-C89 shows motional flexibility on both picosecond-to-nanosecond and possibly millisecond scales |
| 1.20.99.1 | solution structure of enzyme in complex with thioarsenate represents the transiently formed intermediate during the intermolecualr thiol-disulfide exchange reaction. Substantial conformational changes are coupled to the reaction process |
| 1.20.99.1 | wild-type and mutant R60K and R60A enzymes in complex with product arsenite, X-ray diffraction structure determination and analysis at 1.3-1.8 A resolution |
| 1.20.99.1 | X-ray diffraction structure determination and analysis of 2 different crystal forms at 1.64-2.03 A using multiple isomorphous replacement with anomalous scattering and multiple-wavelength anomalous dispersion methods |
