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Results 1 - 6 of 6
EC Number Crystallization (Commentary) Reference
Show all pathways known for 5.1.1.13Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.13catalytically inactive mutant C82A in complex with citric acid, 2.0 A resolution. Citric acid binds to the catalytic site, which induces a conformational change to close the active site. Residue R48 is responsible for recognizing carboxyl groups of the substrates L-/D-aspartates and stabilizing a reaction intermediate, and L164 is responsible for stabilizing a closed state structure 695052
Show all pathways known for 5.1.1.13Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.13purified enzyme, sitting drop vapour diffusion method with microseeding, mixing of 0.002 ml of 20 mg/ml protein in 50 mM MES, pH 6.5, and 4 mM dithiothreitol, with 0.002 ml of reservoir solution containing 25% v/v PEG MME 550, and 5% v/v 2-propanol, and 0.1 M sodium acetate, pH 4.8, equilibration againat 0.1 ml reservoir solution, 20°C, single rod-shaped crystals, X-ray diffraction structure determination and analysis at 2.55 A resolution, molecular replacement calculations are carried out using the coordinates of PhAspR, PDB ID 1jfl, as a starting model 746649
Show all pathways known for 5.1.1.13Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.13purified recombinant enzyme, vapour diffusion method, mixing of 8-12 mg/ml protein in 50 mM Tris-HCl, pH 8.0, with reservoir solution containing 20-25% w/v PEG 3400, 200 mM potassium/sodium tartrate, and 1 mM L-aspartate, X-ray diffraction structure determination and analysis at 1.85 A resolution, molecular replacement method using the structure of aspartate racemase from Salmonella typhimurium, PDB ID 3S81, as a probe model 747720
Show all pathways known for 5.1.1.13Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.13purified recombinant His-tagged enzyme, hanging drop vapour diffusion method, mixing of 0.006 ml of 2.5 mg/ml protein in 10 mM Tris-HCl, 20 mM pyridoxal 5'-phosphate, 1 mM 2-mercaptoethanol, pH 8.8, with 0.003 ml of reservoir solution containing 27% w/v PEG 4000, 50 mM sodium acetate, pH 5.0, 200 mM ammonium acetate, and 15% v/v glycerol, and equilibration against 0.1 ml of reservoir solution, 14°C, X-ray diffraction structure determination and analysis at 1.90 A resolution 746669
Show all pathways known for 5.1.1.13Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.13sitting drop vapour diffusion method at 293 K, space group P21 with a: 65.5 A, b: 58.7 A, c: 67 A and beta 109.6° 652886
Show all pathways known for 5.1.1.13Display the word mapDisplay the reaction diagram Show all sequences 5.1.1.13sitting drop vapour diffusion method at 293 K, space groups: P21 with a: 65.5 A, b: 58.7 A, c: 67.0 A, and beta: 109.6°, P212121 with a: 68.1 A, b: 135 A and c: 151.5 A, and P3121 with a and b: 80.6 A and c: 70.3 A 649148
Results 1 - 6 of 6