EC Number |
Reference |
---|
2.7.4.22 | apo-form UMPK, 2.35 A resolution, crystallisation is significantly improved in a strong magnetic field, buffer-screening procedure, 20 mM N-(2-acetamido)-2-iminodiacetic acid (ADA) pH 6.8, 5 mM beta-mercaptoethanol and 0.02% NaN3, sitting-drop vapour diffusion in 96-well plates, 100 K, monoclinic space group P212121, unit-cell paramerters a = 111.45, b = 120.07, c = 125.79A |
690286 |
2.7.4.22 | bound to the UMP substrate, resolved at 2.3 A resolution, bound to the UDP product, resolved at 2.6 A resolution, bound to UTP, resolved at 2.45 A resolution |
665637 |
2.7.4.22 | complexed with GTP, hanging drop vapor diffusion method, using 150 mM sodium acetate pH 4.8, 270 mM ammonium sulfate, 18% (w/v) PEG MME 550. Complexed with UDP, hanging drop vapor diffusion method, using 0.15 M sodium acetate pH 4.8, 0.35 M ammonium sulfate, 28% (w/v)PEG MME 550 |
721169 |
2.7.4.22 | D159N, hanging drop vapor diffusion method |
698858 |
2.7.4.22 | of the apo-form, crystallization improves by a strong magnetic field, optimum buffer for solubilization is 20 mM N-(2-acetamido)iminodiacetic acid, pH 6.8, 0.02% NaN3 and 5 mM 2-mercaptoethanol |
671130 |
2.7.4.22 | purified recombinant enzyme in complex with ATP, 300 nl sitting drops containing 1.5 mg/mL purified protein are mixed with 3.3 mM ATP, 0.33 mM MgCl2, 66 mM Li2SO4, 3% PEG 3000, 33 mM imidazole, pH 8.0, and 20 mM spermine tetrahydrochloride, equilibration against a reservoir solution of 200 mM Li2SO4, 10% PEG 3000, and 100 mM imidazole, pH 8.0, cryoprotection in 70% reservoir solution with 30% glycerol, 2 days, X-ray diffraction structure determination and analysis at 2.82 A resolution |
693652 |
2.7.4.22 | purified recombinant enzyme, X-ray diffraction structure determination and analysis at 2.5 A resolution |
692284 |
2.7.4.22 | purified recombinant SeMet-substituted apo-enzyme XC1936, crystallization in a strong magnetic field, protein in 5 mM 2-mercaptoethanol, 100 mM N-(2-acetamido)-2-iminodiacetic acid, pH 6.8, and 0.02% NaN3, optimization of the reservoir solution, 25°C, X-ray diffraction structure determination and analysis at 2.35 A resolution |
671130 |
2.7.4.22 | purified recombinant UMP kinase mutant D159N, bound to GTP, by hanging drop vapour diffusion method, 0.004 ml of protein solution containing 4 mg/ml UMPK mutant in 50 mM Tris-HCl, pH 8.0, and 100 mM NaCl, mixed with 0.004 ml precipitant solution containing 22.5 mM GTP and 21.5% w/v PEG 400 in 100 mM sodium acetate, pH 4.6, equilibration against reservoir solution containing 43% PEG 400, 20°C, X-ray diffraction structure determination and analysis at 2.8-3.0 A resolution, molecular replacement and structure modelling |
698858 |
2.7.4.22 | resolved at 2.4 A resolution. Complexed with AMP-PNP, resolved at 3 A resolution. Complexed with AMP-PNP and UMP, resolved at 2.55 A resolution |
666054 |