EC Number   |
|---|
    2.7.2.4 | 3C20, 14% PEG4000, 0.1 M Tris, 0.8 M ammonium formate, pH 8.0, vapor diffusion, hanging drop, temperature 293 K, space group C2221, 3C1N, 0.2 M ammonium iodide, 2.2 M ammonium sulfate, pH 5.0, vapor diffusion, hanging drop, temperature 293 K, space group P212121, 3C1M, 14% PEG4000, 100 mM Tris, 800 mM ammonium formate, pH 8.0, vapor diffusion, hanging drop, temperature 293 K, space group P212121, the structure is determined under three different transition states: ternary complex with MgAMP-PNP and L-aspartate, binary complex with L-aspartate, and binary complex in the presence of its allosteric inhibitor L-threonine |
| 2.7.2.4 | by hanging-drop vapor-diffusion method, in the presence of L-aspartate and MgADP, to 2.822.69 A resolution, N-terminal catalytic domain (residues 2-300) and a C-terminal regulatory domain (residues 310-470) joined through a hinge region (residues 301-309) |
| 2.7.2.4 | by hanging-drop vapour-diffusion method, regulatory subunit in the presence of the inhibitor threonine, to 2.15 A resolution, crystal belongs to the cubic space group P4332 or P4132, with unit-cell parameters a = b = c = 141.8 A |
| 2.7.2.4 | by sitting drop vapor-diffusion method, AKIII in the inactive T-state with bound feedback allosteric inhibitor L-lysine, to 2.8 A resolution, and in the R-state with L-aspartate and ADP, to 2.5 A resolution, unusual configuration for the regulatory ACT domains, in which ACT2 is inserted into ACT1 rather than the expected tandem repeat |
| 2.7.2.4 | by the hanging-drop vapor-diffusion method, crystal structure of the regulatory subunit of AK at 1.58 A resolution in the Thr-binding form, regulatory subunit contains two ACT domain motifs per monomer and is arranged as a dimer, regulatory subunit is a monomer in the absence of Thr but becomes a dimer by adding Thr |
| 2.7.2.4 | by the hanging-drop vapour-diffusion method using Crystal Screen kits, the regulatory subunit (the beta subunit of Thermus thermophilus AK) is crystallized in the presence of the inhibitor threonine. Diffraction data are collected to 2.15 A at a synchrotron source. The crystal belongs to the cubic space group P4332 or P4132, with unit-cell parameters a = b = c = 141.8 A. |
| 2.7.2.4 | crystal structure of the regulatory subunit of aspartate kinase from Mtb alone and in complex with threonine are determined at resolutions of 2.6 A and 2.0 A, respectively. MtbAKbeta is composed of two perpendicular non-equivalent ACT domains (aspartate kinase, chorismate mutase, and TyrA (prephenate dehydrogenase)) per monomer. Each ACT domain contains two alpha helices and four antiparallel beta strands |
| 2.7.2.4 | crystal structures analysis, overview |
| 2.7.2.4 | enzyme free or in complex with L-threonine, hanging drop vapor diffusion method, using 0.1 M sodium acetate (pH 5.0) and 1.2-2.0 M NaCl |
| 2.7.2.4 | hanging drop vapor diffusion method, using 0.4 M ammonium sulfate, 0.1 M sodium citrate tribasic dihydrate (pH 5.6) and 0.9 M lithium sulfate monohydrate |
