EC Number   |
Reference |
|---|
    6.3.1.5 | - |
954 |
| 6.3.1.5 | 28 mg/ml purified recombinant enzyme, pure or in complex with substrates NAD+ and ATP, hanging-drop vapour diffusion method, 22°C room temperature, protein in 0.01 M HEPES, pH 7.5, 5 mM MgCl2, 3 mM DTT, precipitant solution: 0.1 M HEPES, pH 7.5, 1.5 M lithium sulfate, X-ray diffraction structure determination at 2.0 A resolution, compex structure determination via molecular replacement method |
653053 |
| 6.3.1.5 | crystal structures of apo- and complex forms with deamido-NAD+ and ATP to a resolution of 2.3 and 1.7 respectively. Hanging drop vapor diffusion method. Crystals of SeMet-containing NAD+ synthase belong to space group C2 with unit cell dimensions of a = 92.3, b = 47.5, c = 64.0, and beta = 110°. Crystals of NAD+ synthetase complexed with deamido-NAD+ belong to space group P3(1), with unit cell dimensions of a = b = 63.4, c = 125.7 A |
663361 |
| 6.3.1.5 | crystal structures of the enzyme alone and in complex with natural substrates and with the reaction product NAD+ |
662353 |
| 6.3.1.5 | enzyme in complex with ATP, ATP-Tl+, ATP-Mn2+, or NAD-adenylate, hanging-drop vapour diffusion method, 15 mg/ml protein, 5 mM ATP, 20 mM NAD+ in 0.1 M sodium acetate, pH 5.2, 22% PEG 400, and 50 mM MgCl2, thallium acetate, or MnCl2 20°C, 24 h before data collection the crystale are soaked in a cryoprotectant buffer, X-ray diffraction structure determination at 1.3 A resolution, structure analysis and modeling |
653920 |
| 6.3.1.5 | free enzyme form at 2.6 A resolution and in a complex with ATP at 2.0 A resolution |
957 |
| 6.3.1.5 | hanging drop vapour diffusion method using 8-12% PEG 8000, 0.505 M ammonium sulfate, 6% glycerol, 100 mM magnesium chloride, 0.05% n-octyl-beta-D-glucopyranoside, 100 mM HEPES, pH 7 |
671062 |
| 6.3.1.5 | purified recombinant detagged enzyme, sitting drop vapor diffusion method, mixing of 30 mg/ml protein in 0.2 M NaCl, 20 mM Tris-HCl, pH 8.0, 1 mM DTT, 5 mM MgCl2, and 5% glycerol, with reservoir solution containing 20% PEG 4000, 0.2 M lithium sulfate, 0.1 M MES, pH 6.0, 23°C, 3 days, method optimization, X-ray diffraction structure determination and analysis at 2.60 A resolution, molecular replacement |
744619 |
| 6.3.1.5 | purified recombinant enzyme complexed with substrates, vapour diffusion method at 5.2 under earth gravity at pH 5.2, and microseeding under space microgravity, the latter in protein solution containing 15 mg/ml protein, 2.5 mM ATP, 5 mM deamido-NAD+, 50 mM Tris, pH 8.5, 50 mM MgCl2, 25% PEG 400 v/v, 9 days, X-ray diffractio structure determination at 1.0 A resolution and analysis of the crystal structures at pH 5.2 and pH 8.5 |
649175 |
| 6.3.1.5 | purified recombinant enzyme, in complex with 4 different substrates: complex I is formed by enzyme and deamido-NAD, complex II is formed by enzyme and ATP, complex III is formed by enzyme, deamido-NAD and ATP, complex is formed by enzyme and substrate analogue alpha,beta-methylene-adenosine triphosphate, crystallization from protein solution: 15 mg/ml protein, 20 mM sodium acetate, pH 5.2, 50 mM MgCl2, 2.5 mM 2-mercaptoethanol, plus equal volume of 0.1 M sodium acetate, pH 5.2, 21-23% PEG 400, 50 mM MgCl2, at room temperature, addition of substrates at different concentrations, formation of complex IV at different pH-values, in the reservoir solution: 50 mM HEPES, pH 7.5, 0.1 M MgCl2, 20-26% PEG 400, 2 mM AMP-CPP, X-ray diffraction structure determination at resolution 1.9-2.3, structure analysis |
649168 |
