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Results 1 - 10 of 47 > >>
EC Number Crystallization (Commentary)
Show all pathways known for 2.5.1.18Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.18AtuGSTH1-1 in complex with inhibitor S-(4-nitrobenzyl)-glutathione, hanging drop vapor diffusion method, mixing of 0.002 ml of 4.85 mg/ml protein in 15 mM Tris-HCl, pH 7.0, and 10 mM S-(4-nitrobenzyl)-glutathione, with 0.002 ml of well solution 1.4 M Na/K phosphate, pH 8.3, equilibration against 0.8 ml well solution, 16°C, X-ray diffraction structure determination and analysis at 1.4 A resolution
Show all pathways known for 2.5.1.18Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.18complexed with glutathione or its analogues
Show all pathways known for 2.5.1.18Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.18crystals belong to the triclinic space group P1, with unit-cell parameters a = 72.7, b = 74.0, c = 88.6 A, alpha = 79.1°, beta = 80.1°, gamma = 81.5°, likely contains four homodimers per asymmetric unit
Show all pathways known for 2.5.1.18Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.18dmGSTD10 in apo- and glutathione-bound form, and dmGSTD1, hanging drop vapor diffusion method, mixing of 0.002 ml of 10 mg/ml protein in 50 mM Tris-HCl, pH 7.5, with 0.002 ml of reservoir solution16 and 23°C, X-ray diffraction structure determination and analysis, attempts to crystallize dmGSTD1 apo-form are unsuccessful due to its affinity toward glutathione ligand
Show all pathways known for 2.5.1.18Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.18enzyme in complex with GSH is determined at 2.4 A
Show all pathways known for 2.5.1.18Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.18enzyme in complex with substrates glutathione or 1-chloro-2,4-dinitrobenzene, sitting-drop vapour-diffusion method, 0.004 ml of protein solution, containing 20 mM Tris-HCl, pH 7.9, 200 mM NaCl, 2 mM DTT, is mixed with 0.004 ml of reservoir solution containing 6% Tacsimate, pH 8.0, and 26% w/v PEG 3350, for cocrystallization, the protein solution is mixed with glutathione at a molar ratio of 1:1 and with 1-chloro-2,4-dinitrobenzene at a molar ratio of 1:5. The glutathionecomplex crystals from 7% Tacsimate, pH 8.0, 24% w/v PEG 3350 and the CDNB-complex crystals from 8.5% Tacsimate, pH 8.0, 25% w/v PEG 335. Equilibration over 0.5 ml reservoir solution, 22°C, 3 days, X-ray diffraction structure determination and analysis at 2.2 A and 2.0 A resolution, respectively
Show all pathways known for 2.5.1.18Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.18enzyme in GSH-free and -bound forms, using 20% (w/v) PEG8000, 100 mM HEPES-HCl (pH 7.5), 200 mM ammonium sulfate, and 20% (v/v) 2-propanol at 4°C
Show all pathways known for 2.5.1.18Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.18hanging drop vapor diffusion method
Show all pathways known for 2.5.1.18Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.18hanging drop vapor diffusion method, using 0.1 M HEPES pH 7.5, 20% (w/v) PEG 4000, 10% (v/v) 2-propanol, 2 mM GSH, 10 mM dithiothreitol
Show all pathways known for 2.5.1.18Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.18hanging drop vapor diffusion method, using 0.1 M Tris-HCl pH 7.5, 25% (w/v) PEG 4000, 2 mM GSH, and 10 mM dithiothreitol
Results 1 - 10 of 47 > >>