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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant apo, Mn-bound and Fe-bound enzyme, in presence of PEG, 2-3 days, X-ray diffraction structure determination and analysis at 1.56 A, 1.35 A, and 1.48 A, respectively
purified recombinant enzyme by hanging drop vapour diffusion method, 6.5 mg/ml protein in a solution containing 0.1 M Tris-HCl, 1.4 M sodium citrate pH 8.5, 18°C, few days, X-ray diffraction structure determination and analysis at 1.7 A resolution
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
MnSOD-2 and MnSOD-3, at 3 and 8 mg/ml respectively, in 10 mM Tris-HCl, pH 7.8, mixing of 0.001 ml protein and reservoir solution, the latter containing 0.1 M bicine pH 9.2 and 3.0 M ammonium sulfate for MnSOD-2, and 0.1 M bicine, pH 9.2, and 2.7 M ammonium sulfate for MnSOD-3, X-ray diffraction structure determination and analysis at 1.7-1.8 A resolution
two different monoclinic crystal forms, both with space group P21. Form 1 contains a homodimer in the asymetric unit, form II contains two homodimers per asymmetric unit. Comparison with isostructural MnSOD of Escherichia coli
recombinant His6-tagged enzyme, hanging drop vapor diffusion method, 10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, at 23°C, mixing of 0.001 ml protein solution with 0.001 ml precipitant solution containing 1.9 M ammonium sulfate in 0.2 M Tris-HCl buffer, pH 8.0, X-ray diffraction structure determination and analysis at 2.4 A resolution, modelling
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
from recombinant Mn-SOD, asymmetric unit, hanging drop technique, room temperature, equilibration of 3-4 mg/ml enzyme in ammonium phosphate, pH 5.9, plus 10% 2-methyl-2,4-pentanediol against 32% 2-methyl-2,4-pentanediol, X-ray analysis
mutant enzymes F66A and F66L, hanging drop vapor diffusion method, 0.005 ml of enzyme solution are mixed with 0.005 ml of precipitant solution containing 2.5 M ammonium sulfate, 100 mM imidazole, and 100 mM malic acid, pH 8.5, equilibration against 1 ml of precipitant solution, 1 week, room temperature, X-ray diffraction structure determination and analysis at 2.2 A and 2.3 A resolution, respectively
purified enzyme MnSOD in complex with azide, hanging-drop vapor diffusion, mixing of 0.001 ml of 21 mg/ml protein solution with 0.001 ml of reservoir solution 1.8 M potassium phosphate, pH 7.8, at room temperature for1 day, to obtain the azide complex, 0.002 ml of reservoir containing 200 mM sodium azide are added to drops of 6 day crystals, X-ray diffraction structure determination and analysis at 1.77-1.82 A resolution
purified recombinant SOD1, hanging drop vapour diffusion, 0.001 ml of 10 mg/ml protein in 50 mM sodium citrate, pH 5.5, 1 mM DTT, 100 mM CuSO4, and 100 mM ZnSO4, is mixed with 0.001 ml of reservoir solution containing 21-25% w/v PEG 4000, 0.1 M sodium acetate, pH 4.2-5.2, X-ray diffraction structure determination and analysis at 3.5 A, molecular replacement
purified zinc-deficient mutant enzyme, 0.002 ml of solution containing 15.7 mg/ml protein in 50 mM Na/K phosphate, pH 7.7, is mixed with 0.002 ml of reservoir solution containing 2.45 M ammonium sulfate, 200 mM NaCl in 50 mM Tris, pH 7.5, room temperature, less than 1 week, X-ray diffraction structure determination and analysis at 2.0 A resolution, modelling
recombinant human Cu,Zn-SOD expressed in yeast, hanging drop method by vapour diffusion from 50 mM phosphate, pH 7.7, resulting in 3 different crystal forms
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
purified recombinant enzyme, two different crystal forms, 15 mg/ml protein, mixing of equal volumes of 0.002 ml of protein and reservoir solution, from 1.8 M ammonium sulfate, 00.1 M NaCl, 100 mM FeCl3, 100 mM HEPES, pH 7.0, and 3% v/v isopropanol, at 20°C, mixing of equal volumes of protein and reservoir solution, 3-5 days, X-ray diffraction structure determination and analysis at 2.1 A resolution, molecular replacement
purified mutant enzyme Y41F, hanging drop vapor diffusion method, 21°C, 1:1 mix of the reservoir solution containing 8% PEG 8000, 0.1 M Tris-HCl, pH 8.5, and the protein solution containing 1.45 mg/mL Y41F, 20 mM Tris-HCl, pH 7.8, and 1% glycerol, X-ray diffraction structure determination and analysis
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
purified enzyme, hanging drop vapor diffusion method, 20°C, mixing of 0.003 ml of the concentrated protein solution with 0.003 ml of the reservoir solution containing 16.25% PEG 4000, 0.2 M ammonium sulfate, 5% w/v 2-propanole, 0.1 M HEPES, pH 7.5, X-ray diffraction structure determination and analysis at 2.5 A resolution
purified recombinant enzyme, hanging-drop vapour-diffusion, 0.0025 ml of 10.5 mg/ml protein in 20 mM Tris-HCl, pH 8.2, are mixed with 0.0025 ml of reservoir solution containing 1.4 M sodium potassium phosphate, pH 8.2, equilibration against 0.8 ml of reservoir solution, 16°C, 4 days, method screening and optimization, X-ray diffraction structure determination and analysis at 1.9 A resolution