EC Number   |
Reference |
|---|
   3.5.2.6 | - |
209309, 209311, 209346, 698465 |
| 3.5.2.6 | 0.003 ml 10 mg/ml purified recombinant wild-type enzyme or mutant R234K, mixed with 0.001 ml of well solution containing 2 M ammonium sulfate, 50 mM MOPS pH 6.4, and 0.1 M acetate pH 4.5, respectively, 100 mM MgCl2, 1-2 weeks at room temperature, X-ray diffraction structure determination and analysis at 1.75 A resolution |
654597 |
| 3.5.2.6 | 0.98 mg/ml purified mutant N152A in complex with inhibitor moxalactam in 1.7 M potassium phosphate, pH 8.7, 23°C, after microseeding with the wild-type enzyme in 1 M potassium phosphate, pH 8.7, vapor diffusion hanging drop method, serial dilutions, 5-7 days, X-ray diffraction structure determination and analysis at 1.83 A resolution |
654608 |
| 3.5.2.6 | 2.5-3 mg/ml purified recombinant enzyme in 10% PEG 8000, 0.05 M HEPES, pH 7.5, vapour diffusion sitting drop method, equilibration of 0.01 ml protein solution over a reservoir solution containing 20% PEG 8000, macro-seeding at 1.2-1.5 mg/ml, growth of prismatic crystals, X-ray diffraction structure determination and analysis at 1.5 A resolution, modeling |
657300 |
| 3.5.2.6 | as the native enzyme, with Cys221 oxidized, and with a sulfur atom bridging the two active-site zinc ions, to 1.9, 1.8 and 2.5 A resolution, respectively. Comparison with VIM-2 and VIM-4 structures suggests an explanation for the reduced catalytic efficiency of VIM-7 against cephalosporins with a positively charged cyclic substituent at the C3 position. Kinetic variations are attributed to substitutions in residues 6066, that form a loop adjacent to the active site previously implicated in substrate binding, and to the disruption of two hydrogen-bonding clusters through substitutions at positions 218 and 224 |
720256 |
| 3.5.2.6 | BLaC is crystallized in the hanging drop vapor diffusion configuration over well conditions that include 0.1 M HEPES (pH 7.5) and 2 M NH4H2PO4. The final pH of the well solution is 4.1 |
711240 |
| 3.5.2.6 | crystal quality of Toho-1 is improved by using surface modification to remove a sulfate ion involved in crystal packing |
710730 |
| 3.5.2.6 | crystal structure of a BS3-lactivicin complex |
712707 |
| 3.5.2.6 | crystal structure of the complex of SHV-1 mutant D104E with beta-lactamse inhibitor protein BLIP, to 1.6 A resolution. Mutation D104E results in a 1000fold enhancement in binding affinity to BLIP, as it restores a salt bridge to BLIP. Mutation of a neighboring residue, BLIP E73M, results in salt bridge formation between SHV-1 D104 and BLIP K74 and a 400fold increase in binding affinity. BLIP F142 cooperatively stabilizes both interactions |
721004 |
| 3.5.2.6 | crystal structure of wild-type enzyme mutant enzyme N220G, and of the complex of wild-type enzyme with biapenem |
666038 |
