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Results 1 - 10 of 14 > >>
EC Number Crystallization (Commentary)
Display the word mapDisplay the reaction diagram Show all sequences 3.1.3.16-
Display the word mapDisplay the reaction diagram Show all sequences 3.1.3.16coexpression of the human regulatory subunit and the catalytic subunit from Neurospora crassa in cultured insect cells results in formation of large crystals in the cytoplasm
Display the word mapDisplay the reaction diagram Show all sequences 3.1.3.16hanging drop vapour diffusion method with 0.2 M MgCl2, 4.5% PEG 10000 (w/v) and 0.1 M HEPES (pH 7.5)
Display the word mapDisplay the reaction diagram Show all sequences 3.1.3.16hanging drop vapour diffusion method, using 7-10% (w/v) PEG35000 and 0.1-0.15 M sodium citrate (pH 5.5)
Display the word mapDisplay the reaction diagram Show all sequences 3.1.3.16in complex with inhibitor-2 using the sitting drop vapour diffusion method with 100 mM Tris-HCl, pH 7.5, 300 mM potassium acetate, 12% (w/v) polyethylene glycol 3350, or with 100 mM Tris-HCl, pH 8.6, 150 mM sodium citrate, and 20% (w/v) polyethylene glycol 3350
Display the word mapDisplay the reaction diagram Show all sequences 3.1.3.16in complex with nodularin-R and tautomycin, PP1:nodularin-R is crystallized in 20% (w/v) PEG 3350, 0.2 M NaI. PP1:tautomycin is crystallized in 0.1 M Tris pH 8.0, 30% (w/v) PEG 6K, 1M LiCl
Display the word mapDisplay the reaction diagram Show all sequences 3.1.3.16phosphatase KAP
Display the word mapDisplay the reaction diagram Show all sequences 3.1.3.16purified recombinant detagged apo-form of the catalytic subunit, apo-PPZ1cat, or fused to microcystin-LR (the marine toxin microcystin-LR is a potent cyclic peptide inhibitor of PP1), by hanging drop vapor diffusion method, mixing of enzyme in 20 mM Tris, pH 8.0, 500 mM NaCl, 0.5 mM Tris(2-carboxyethyl) phosphine (TCEP), and 1 mM MnCl21.8 M with ammonium citrate tribasic, pH 7.0, in a 1:1 ratio, and subsequent mixture in a 2:1 protein/crystallization condition ratio with reservoir solution containing 0.06 M citric acid, pH 4.1, and 16% w/v PEG 3350, X-ray diffraction structure determination and analysis at 2.4-2.6 A resolution, molecular replacement using PP1 stucture, PDB ID 4MOV, as the search model
Display the word mapDisplay the reaction diagram Show all sequences 3.1.3.16purified recombinant enzyme bound to the regulatory 34 kDa myosin phosphatase targeting subunit MYPT1 residues 1-299, 8 mg/ml protein in 10 mM Tris, pH 7.5, 20 mM NaCl, 4 mM DTT, and 1 mM MnCl2, 20°C, hanging drop vapour diffusion method, mixed with an equal volume of reservoir solution containing 9.2% w/v PEG 5000 monomethylether, 35% v/v glycerol, and 200 mM NH4Cl, X-ray diffraction structure determination and analysis at 2.7 A resolution
Display the word mapDisplay the reaction diagram Show all sequences 3.1.3.16purified recombinant enzyme Tk-PTP(form I) Tk-PTP(form II) Tk-PTP(G95A), sitting-drop vapor diffusion method, for enzyme form I: mixing 0.001 ml of 10 mg/ml protein solution with 0.001 ml of precipitant solution containing 0.1 M sodium citrate, pH 5.4, 8% w/v PEG 10000, and 14% v/v dioxane, for enzyme form II: mixing of mixing 0.001 ml of 10 mg/ml protein solution with 0.001 ml of precipitant solution containing 0.03 M citric acid, 0.07 M Bis-Tris propane, pH 7.6, 8% w/v PEG 3350, and 0.08 M spermine tetrahydrochloride, and for mutant Tk-PTP(G95A): mixing of 0.001 ml of 10 mg/ml protein solution with 0.001 ml of precipitant solution containing 0.1 M Bis-Tris, pH 6.25, and 0.8 M magnesium formate dehydrate, all at 18°C, X-ray diffraction structure determination and analysis at 1.7-2.3 A resolution, molecular replacement method, model building
Results 1 - 10 of 14 > >>