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EC Number
Crystallization
Reference
crystallization is performed by vapor diffusion in hanging drops
crystals are grown at 23°C by vapor diffusion in hanging drops, crystal structures of the enzyme in its binary complexes with the substrate phosphoenolpyruvate and with a mechanism-based inhibitor
data reading at -173°C
purified recombinant enzyme, hanging-drop vapor diffusion method, mixing of 300 nl of 10 mg/ml protein in 30 mM Tris-HCl, pH 8.0, 200 mM NaCl with 300 nl reservoir solution containing 28% v/v PEG 400, 0.1 M HEPES, pH 7.5, and 0.2 M CaCl2, X-ray diffraction structure determinatin and analysis; purified recombinant enzyme, hanging-drop vapor diffusion method, mixing of 300 nl of 10 mg/ml protein in 30 mM Tris-HCl, pH 8.0, 200 mM NaCl with 300 nl reservoir solution containing 28% v/v PEG 400, 0.1 M HEPES, pH 7.5, and 0.2 M CaCl2, X-ray diffraction structure determinatin and analysis
purified recombinant His-tagged wild-type and mutant H204A enzymes in apoform, or wild-type enzyme complexed with Zn2+ or Cd2+, hanging drop vapor diffusion method, mixing of 0.001 ml of protein solution, containing inhibitor in a 1:2 ratio, with 0.001 ml of reservoir solution, containing 18% PEG 3350, 0.1 M HEPES, pH 7.5, and 0.25 M magnesium chloride hexahydrate, equilibration against reservoir solution, 20°C, 14 days, X-ray diffraction structure determination and analysis at 2.0 A resolution, molecular replacement and modelling
purified recombinant His6-tagged enzyme, sitting drop vapour diffusion method, mixing of 0.003 ml of 5 mg/ml protein in 0.2 M Tris-HCl, pH 7.4, 0.1 M NaCl, 0.05% 2-mercaptoethanol, and 0.1 mM phosphoenolpyruvate with 0.0015 ml of reservoir solution containing 0.2 M calcium acetate, 0.1 M sodium cacodylate, pH 6.5, 18% w/v PEG 8000, 20°C, 2 days, X-ray diffraction structure determination and analysis at 2.8 A resolution, molecular replacementusing structure PDB ID 1g7v and model building
purified recombinant mutant enzymes, hanging-drop vapor diffusion, mixing of 0.002 ml of protein solution containing 20 mg/ml protein in 10 mM BTP, pH 7.5, with 0.002 ml of reservoir solution containing 100 mM sodium acetate, pH 4.6, and 0.6-3.0 M NaCl, equilibration against 0.5 ml reservoir solution, 20°C, 24 h, X-ray diffraction structure determination and analysis at 1.75-2.10 A resolution
structure of the metal-free and Cd2+ forms of the enzyme are determined in the uncomplexed state and in complex with various combinations of phosphoenolpyruvate, arabinose 5-phosphate and erythrose 4-phosphate
structures of apo-enzyme and of binary complexes with the substrates phosphoenolpyruvate, the product 2-dehydro-3-deoxy-D-octonate 8-phosphate and the catalytically inactive 1-deoxy analog of arabinose 5-phosphate
Results 1 - 10 of 13 > >>