EC Number |
Reference |
---|
2.7.1.30 | - |
641286, 641294, 641295, 641299, 641300, 641317, 641327, 702293, 705779 |
2.7.1.30 | crystals are grown at 20°C by the sitting-drop vapour diffusion method. Native X-ray diffraction data are collected to 2.4 A resolution using synchrotron radiation at station BL44XU of SPring-8. The crystal belongs to the rhombohedral space group R3, with unit-cell parameters a = b = 217.48, c = 66.48 A. The protein is also cocrystallized with substrates and diffraction data are collected to 2.7 A resolution |
684168 |
2.7.1.30 | crystals are obtained by the hanging-drop technique from a solution containing 29% polyethylene glycol 400, 0.1 M sodium acetate pH 4.5, 0.1 M calcium acetate and 10% glycerol. The crystals can grow in the presence of 33% PEG 400, which allows to mount the crystals and directyl flash-cool them. Repeated flash-annealing causes a significant decrease in the averaged mosaicity along with an increase in the overall peak counts of reflections and an enhanced signal-to-noise ratio. Individual reflection-profile analysis reveales a mostly dual domain structure, showing the minimization of one domain as a result of flash-annealing. |
677308 |
2.7.1.30 | crystals of native and mutant enzyme with bound glycerol, hanging drop vapor diffusion method |
661122 |
2.7.1.30 | in complex with glycerol, ADP and the allosteric effector enzyme IIAGlc |
661122 |
2.7.1.30 | in complex with glycerol, in presence and absence of fructose 1,6-diphosphate, mechanism |
641326 |
2.7.1.30 | in complex with substrates, sitting drop vapor diffusion method, using M HEPES pH 7.5, 11% (v/v) hexane-1,6-diol, 25% (w/v) PEG400 |
739102 |
2.7.1.30 | of wild type and mutant A65T, both in complex with glycerol and ADP, and of mutant I474D, in complex with IIAGlc |
641320 |
2.7.1.30 | purified recombinant His6-tagged enzyme in complex with pNPP, sitting drop method, mixing of 0.001 ml of 5 mg/mL TbgGK in 10 mM MgSO4, 20 mM NaCl, 0.001% glycerol and 10 mM MOPS, pH 6.8, with 0.001 ml of 11% 1,6-hexanediol, 25% PEG 400, and 0.1 M HEPES, pH 7.5, at 20°C, crystals of the TbgGK-pNPP complex are obtained by soaking TbgGK crystals in a cryoprotectant solution containing 5.5% 1,6-hexanediol, 40% PEG 400, and 0.1 M HEPES, pH 7.5, that is supplemented with 20 mM pNPP, at 20°C, for 6-14 h, X-ray diffraction structure determination and analysis, molecular replacement method using the protein structure of the TbgGK-ADP complex (PDB ID 3WXL) as a search model |
760620 |
2.7.1.30 | purified recombinant wild-type enzyme in complex with glycerol and AMPPCP, and enzyme mutant K271E free or in complex with glycerol, sitting drop vapor diffusion method, 4-5 mg/ml protein in 5 mM Tris-HCl, pH 7.5, with or without 5 mM glycerol, and 5 mM AMPPCP, is mixed with 0.1 M HEPES, pH 8.0, containing 15% w/v PEG 1000 and 200 mM calcium acetate, 20°C, X-ray diffraction structure determination and analysis at 2.3-3.1 A resolution, molecular replacement using the structure of Tk-GK (PDB ID 2ZF5) as template, modelling |
761561 |