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Results 1 - 8 of 8
EC Number Crystallization (Commentary) Reference
Show all pathways known for 5.4.99.16Display the word mapDisplay the reaction diagram Show all sequences 5.4.99.16crystals are grown by vapor diffusion. Structure of the Mycobacterium smegmatis TreS:Pep2 complex, containing trehalose synthase (TreS) and maltokinase (Pep2), which converts trehalose to maltose 1-phosphate as part of the TreS:Pep2-GlgE pathway. The structure, at 3.6 A resolution, reveals that a diamond-shaped TreS tetramer forms the core of the complex and that pairs of Pep2 monomers bind to opposite apices of the tetramer in a 4 + 4 configuration 759499
Show all pathways known for 5.4.99.16Display the word mapDisplay the reaction diagram Show all sequences 5.4.99.16enzyme complexed with alpha-acarbose, Ca2+, Cl-, and Mg2+ or with Cl-, Ca2+, and Mg2+, PDB IDs 3ZOA and 3ZO9, X-ray diffraction structure determination and analysis at 1.85 and 1.84 A resolution, respectively 746863
Show all pathways known for 5.4.99.16Display the word mapDisplay the reaction diagram Show all sequences 5.4.99.16enzyme complexed with Ca2+, glycerin, and sulfate ion, PDB ID 4LXF, X-ray diffraction structure determination and analysis at 2.6 A resolution 746863
Show all pathways known for 5.4.99.16Display the word mapDisplay the reaction diagram Show all sequences 5.4.99.16enzyme complexed with Ca2+, Mg2+, and tromethamine, PDB ID 4TVU, X-ray diffraction structure determination and analysis at 2.7 A resolution 746863
Show all pathways known for 5.4.99.16Display the word mapDisplay the reaction diagram Show all sequences 5.4.99.16enzyme, PDB ID 5X7U, X-ray diffraction structure determination and analysis at 2.5 A resolution 746863
Show all pathways known for 5.4.99.16Display the word mapDisplay the reaction diagram Show all sequences 5.4.99.16free enzyme and enzyme in complex with inhibitor acarbose, hanging drop vapor diffusion technique, mixing of 0.002 ml of 20 mg/ml protein in 40 mM sodium phosphate buffer, pH 6.0, with 0.002 ml of reservoir solution containing 0.1 M sodium cacodylate, pH 6.5, 0.2 M MgCl2, and 10-14% PEG 1000, 20°C, 1 day to 1 week, X-ray diffraction structure determination and analysis at 1.84 A resolution, molecular replacement 727598
Show all pathways known for 5.4.99.16Display the word mapDisplay the reaction diagram Show all sequences 5.4.99.16purified recombinant enzyme mutant N253F, hanging drop vapour diffusion method, mixing of 0.002 ml of 30 mg/ml protein in 20 mM HEPES, pH 7.5, 100 mM NaCl, 3.3% glycerol, and 1 mM DTT, with 0.0.02 ml of reservoir solution containing 0.3 M Tris-HCl pH 7.0, 7% PEG 4000, and 0.2 M sodium acetate trihydrate, and equilibration against 0.5 ml of reservoir solution, 15°C, 2-3 weeks, X-ray diffraction structure determination and analysis 746668
Show all pathways known for 5.4.99.16Display the word mapDisplay the reaction diagram Show all sequences 5.4.99.16purified recombinant wild-type and N253A mutant enzymes in complex with inhibitor Tris, hanging drop vapour diffusion method, 15°C, for the wild-type enzyme, mixing of 0.002 ml of 30 mg/ml protein in 20 mM sodium phosphate, pH 7.4, with 0.002 ml of reservoir solution containing 9% PEG 4000, 0.2 M sodium acetate trihydrate, 0.3 M Tris-HCl, pH 8.5, 6-8 weeks, for the mutant enzyme, mixing of 0.002 ml of 60 mg/ml protein in 20 mM sodium phosphate, pH 7.4, with 0.002 ml of reservoir solution containing 11% PEG 4000, 0.2 M sodium acetate trihydrate, 0.3 M Tris-HCl, pH 8.5, and 5% glycerol, 2 weeks, X-ray diffracion structure determination and analysis at 2.21-2.70 A resolution 746621
Results 1 - 8 of 8