EC Number |
Reference |
---|
1.3.1.10 | FabL in apo form and in the ternary complex with NADP+ and an indole naphthyridinone inhibitor, X-ray diffraction structure determination and analysis |
711113 |
1.3.1.10 | FabL in apo form and in the ternary complex with NADP+ and inhibitor (E)-N-(1,2-dimethyl-1-H-indol-3-ylmethyl)-N-methyl-3-(7-oxo-5,6,7,8-tetrahydro-1,8-naphthyridin-3-yl) acrylamide, 8 mg/ml protein in 20 mM Tris, pH 8.0, 100 mM NaCl, and 1 mM DTT, is mixed with an equal volume of reservoir solution containing 0.1 M sodium citrate pH 5.6, 8% w/v PEG 10,000 and 0.4 M magnesium acetate, hanging-drop methods, for the ternary BcFabL-NADP+-INH complex, NADP+ and inhibitor are added at the molar ratio of 1:1.5 and 1:5, respectively, equilibration in a stabilizing solution containing 0.1 M sodium citrate, pH 5.6, 8% w/v PEG 10,000, 0.4 M magnesium acetate with 30% v/v ethylene glycol as the cryoprotectant, X-ray diffraction structure determination and analysis at 2.2-3.0 A resolution |
711113 |
1.3.1.10 | hanging drop vapour diffusion method with 0.04 M MgCl2, 0.05 M sodium cacodylate pH 6.0 and 11% (v/v) 2-methyl-2,4-pentanediol at 4°C |
684170 |
1.3.1.10 | purified recombinant wild-type enzyme free and in complex with NADPH, mutant enzyme Y79N, hanging drop vapour diffusion method, 22°C, 15-25 mg/ml free enzyme in 50 mM sodium phosphate, pH 7.0, 150 mM NaCl with or without 10 mM NADPH, in a 1:1 ratio with reservoir solution containing 1.9 M ammonium sulfate, and 0.1 M N-(2-acetamido)-2-iminodiacetic acid/NaOH, at pH 6.5 for the free enzyme and pH 7.0 for the cofactor-complexed enzyme, mutant Y79N is crystallized using 15 mg/ml protein and reservoir solution at pH 7.0, labeling by soaking in heavy-atom-solutions, X-ray diffraction structure determination and analysis at 1.7 A, 2.25 A, and 2.6 A, respectively |
656515 |
1.3.1.10 | structure to 1.9 A resolution with endogenous FMN fully resolved and the NADPH cofactor partially resolved. FabK possesses a TIM-barrel motif, and all flexible loops are visible |
762574 |