EC Number   |
|---|
    1.15.1.1 | - |
| 1.15.1.1 | analysis of both solution and crystal structure of superoxide dismutase paralog lacking two Cu ligands and without enzymic activity. In solution, protein is monomeric. In crystal structure, it is well structured and organized in covalent dimers. Discussion of order/disorder transition |
| 1.15.1.1 | asymmetric unit, from Cu,Zn-SOD, sitting drop technique by vapour diffusion, 25 mM citrate, 10 mM phosphate buffer, pH 6.5, 6% w/v polyethylene glycol, stabilization by 35% polyethylene glycol, X-ray analysis, modeling of three-dimensional structure |
| 1.15.1.1 | comparison of native protein and enzyme nitrated at active site residue Y34, no significant change in conformation upon nitration |
| 1.15.1.1 | crystal structures of unfluorinated and fluorinated enzyme are nearly superimposable. Ratio kcat/Km decreases from 0.8 per mM and s for wild-type to 0.03 per mM and s for the fluorinated mutant which is in significant part due to 3-fluorotyrosine residues distant from the active-site metal |
| 1.15.1.1 | dialysis against 0.1 mM EDTA than against water, Mn-SOD |
| 1.15.1.1 | enzyme 10 mg per ml in Tris/HCl 50 mM, pH 8.2 by dialysis against ammonium sulfate 2.8 M, pH 8.2, 4°C |
| 1.15.1.1 | extracellular enzyme, tetraborate crystallization of ethanolic enzyme extract, then recrystallization from buffer than from water |
| 1.15.1.1 | Fe-SOD, dialysis against 55% saturated ammonium sulfate solution, pH 4.5, 1 week at 2°C under reduced pressure |
| 1.15.1.1 | from Cu,Zn-SOD, always twinned, hexagonal crystals with asymmetric units, from 2-methyl-2,4-pentanediol in potassium phosphate buffer, pH 6.5, hanging drop technique by vapour diffusion, X-ray analysis |
