EC Number   |
Reference |
|---|
    1.18.1.3 | ferredoxin reductase component of biphenyl dioxygenase |
437852 |
| 1.18.1.3 | purified recombinant BphA4 in complex with BphA3, anaerobic crystallization is essential to crystallize the productive complex between oxidized BphA3 and NADH-reduced BphA4, sitting-drop vapour-diffusion method, 26.4 mg/ml BphA4 in 50 mM potassium phosphate buffer, pH 7.0, is reduced with 20 mM NADH for 5 min at 4°C, and mixed with oxidized BphA3 at a concentration of 17.5 mg/ml, mixing of 0.9 ml of each of the protein and reservoir solutions, and equilibration against 500 ml reservoir solution, containing 0.2 M ammonium acetate, 0.1 M sodium citrate, pH 5.6, 30% w/v PEG 4000, 20°C, X-ray diffraction structure determination and analysis at 1.9 A resolution |
684179 |
| 1.18.1.3 | purified recombinant enzyme, hanging-drop vapour-diffusion method, 0.001 ml of protein solution with 20mg/ml protein in 20 mM HEPES, pH 7.0, and 0.001 ml reservoir solution, containing 100 mM HEPES, pH 7.0-7.2, 16-18% w/v PEG 10 000 at 18°C, are mixed and equilibrated against 200 ml reservoir solution, 70 mM sodium cacodylate pH 6.5, 0.98 M sodium acetate, 30% v/v glycerol are best for cryoprotection, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular replacement using the putidaredoxin reductase structure, overview |
684177 |
| 1.18.1.3 | recombinant His-tagged RedIIA from KA1, hanging-drop vapour-diffusion, 5°C, method using PEG 4000, X-ray diffraction structure determination and analysis at 1.58 A resolution, modelling |
706994 |
