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Results 1 - 10 of 10
EC Number Crystallization (Commentary)
Show all pathways known for 4.1.1.11Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.11-
Show all pathways known for 4.1.1.11Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.11both apo form and in complex with isoasparagine
Show all pathways known for 4.1.1.11Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.11co-crystallization of fully activated PanD and PanZ in complex, in a 10:11 PanD:PanZ ratio (protomer to monomer), hanging drop vapor diffusion method, mixing of 0.003 ml of 9 mg/ml protein in 50 mM Tris, 100 mM NaCl, and 0.1 mM DTT, pH 7.5, with 00.001 ml of reservoir solution containing 200 mM KSCN, 100 mM Bis-Tris propane, pH 6.5, and 20% w/v PEG 3350 at 18°C, X-ray diffraction structure determination and analysis at 1.16 A resolution. The same structure is observed using both room-temperature and cryo-cooled crystals, indicating that the hydrate is formed from the pyruvoyl cofactor and is not an intermediate in the activation reaction. This state is stabilized by a hydrogen bond to the amide of Gly24, which is held in place by interactions with PanZ
Show all pathways known for 4.1.1.11Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.11crystal structure at 2.2. A resolution
Show all pathways known for 4.1.1.11Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.11crystal structure of an unprocessed native proenzyme and of the mutants G24S, S25A, S25C, S25T, H11A, Ala-24 and Ala-26 insertion mutants, hanging-drop vapour-diffusion method
Show all pathways known for 4.1.1.11Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.11purified recombinant His-tagged unprocessed, native precursor ADC, vapor diffusion hanging drop method, the precipitant solution contains 0.1 M sodium cacodylate, pH 6.5, 1.5 M magnesium sulfate, and 20% w/v PEG 2000, 15 days, cryoprotection by 20% v/v glycerol, X-ray diffraction structure determination and analysis at 2.99 A resolution
Show all pathways known for 4.1.1.11Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.11purified recombinant mutant N72A, hanging drop vapour diffusion method, mixing of 0.001 ml of 19 mg /ml protein in 50 mM Tris-HCl, pH 8.0, with 0.001 ml of reservoir solution containing 1.6 M ammonium sulfate, pH 4.0, and equilibration against 0.5 ml of reservoir solution, 19°C, 3 days, cryoprotection by 1.8 M ammonium sulfate, 0.1 M citric acid, 30% glycerol pH 4.0 using 5% increments in glycerol concentration to prevent crystal dissolution, X-ray diffraction structure determination and analysis at 1.7 A resolution
Show all pathways known for 4.1.1.11Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.11purified recombinant protein complex PanD-PanZ-AcCoA, protein complexes are prepared with a 10:11 ratio of PanD to PanZ at a total protein concentration of 9-11 mg/ml, and a 2fold molar excess (with respect to PanZ) of acetyl-CoA. Crystals are obtained in 20% w/v PEG 3350, 0.1 M Bis-Tris propane, pH 7.4, and 0.2 M potassium thiocyanate, X-ray diffraction structure determination and analysis at 1.6 A resolution
Show all pathways known for 4.1.1.11Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.11purified recombinant T57V mutant enzyme, hanging drops by vapour diffusion with a 1:1 ratio of protein to precipitant, 7.5 mg/ml protein, 1.5-3.4 M sodium malonate, pH 4.0, method optimization, 17°C, X-ray diffraction structure determination and analysis at 1.62 A resolution, modeling
Show all pathways known for 4.1.1.11Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.11recombinant enzyme in the presence of the substrate analogue isoasparagine, hanging-drop vapour-diffusion method, X-ray analysis
Results 1 - 10 of 10