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Results 1 - 4 of 4
EC Number Crystallization (Commentary) Reference
Show all pathways known for 2.7.1.100Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.100ADP-2Ho and ADP-2Mg complexes 671059
Show all pathways known for 2.7.1.100Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.100purified recombinant His-tagged enzyme, hanging drop vapour diffusion method, 0.002 ml of protein solution containing 10 mg/ml protein in 20 mM imidazole, pH 7.6, 2 mM DTT, 1 mM 5-methyl-5-thio-D-ribose and 1 mM ATP-gamma-S, is mixed an equal volume of reservoir solution containing 10% w/v PEG 8000, 0.1 M sodium cacodylate, pH 6.5, and 0.2 M magnesium acetate, equilibration against 0.5 ml reservoir solution, room temperature, 3 days, cryoprotection by soaking in reservoir solution plus 25% v/v ethylene glycol, X-ray diffraction structure determination and analysis at 1.9 A resolution, identification of heavy-atom derivatives 660580
Show all pathways known for 2.7.1.100Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.100purified recombinant non-tagged enzyme, hanging drop vapour diffusion method, 0.002-0.003 ml of protein solution containing 7.5-15 mg/ml protein in 10 mM potassium phosphate, pH 7.4, 2 mM DTT, 1 mM 5-methyl-5-thio-D-ribose and 1 mM ATP-gamma-S, or 8 mM CHAPS, is mixed an equal volume of reservoir solution containing 22% w/v PEG 2000 monomethylether, 0.1 M Tris-HCl, pH 7.5, and 0.3 M sodium acetate, equilibration against 0.5 ml reservoir solution, room temperature, 3 days, cryoprotection by soaking in reservoir solution plus 25% v/v ethylene glycol, X-ray diffraction structure determination and analysis at 3.0 A resolution without detergent, and at 2.2 A resolution in presence of CHAPS, no crystallization of His-tagged enzyme possible, identification of heavy-atom derivatives 660580
Show all pathways known for 2.7.1.100Display the word mapDisplay the reaction diagram Show all sequences 2.7.1.100structure determination, 1.9 A resolution, diffraction data and crystallographic refinement statistics, similarity to enzyme structure of Bacillus subtilis, conformation of Gly-rich loop more extended in Arabidopsis thaliana than in bacterial enzyme homologues, different conformations of G-loops and W-loops in Arabidopsis thaliana and Bacillus subtilis enzymes despite of high sequence similarities, significant ATPase activity in the absence of 5-methyl-5-thio-D-ribose suggested, features of the substrate binding site offer opportunities for a simple organic salt of a 5-methyl-5-thio-D-ribose analog to specifically inhibit kinase activity 691517
Results 1 - 4 of 4