EC Number   |
Reference  |
|---|
   1.14.20.1 | crystallization of wild-type enzyme and of the DELTAR306 mutant complexed with iron(II) and 2-oxoglutarate to 2.1 A and the DELTAR306A mutant complexed with iron(II), succinate and unhydrated carbon dioxide to 1.96 A |
440368 |
| 1.14.20.1 | recombinant enzyme expressed in Escherichia coli, high-resolution structures for apoenzyme, the enzyme complexed with Fe(II), and with Fe(II) and 2-oxoglutarate |
440369 |
| 1.14.20.1 | hanging drop method, recombinant enzyme expressed in Escherichia coli |
440373 |
| 1.14.20.1 | recombinant N-terminally His-tagged wild-type and C-terminally truncated mutant enzymes, free enzyme, or complexing with Fe2+, or Fe2+/ampicillin, hanging drop vapour diffusion method, 4°C, precipitant solution: 100 mM HEPES-NaOH, pH 8.0, 0.9-1.1 M ammonium sulfate, the reservoir solution is covered with oil to retard the evaporation, cryoprotection by 30% v/v ethylene glycol in precipitant solution, X-ray structure determination and analysis at 2.3 A resolution, molecular modeling |
659719 |
| 1.14.20.1 | quantum mechanical calculations of the first part of the reaction based on the high-resolution structures of the active site and its complexes with ligands |
687191 |
| 1.14.20.1 | as apoprotein with N-terminal His tag, 2.3 A resolution |
699366 |
| 1.14.20.1 | as apoprotein, 1.3 A resolution |
699366 |
| 1.14.20.1 | crystallization of mutant delta R306, with Fe2+ and 2-oxoglutarate, 2.1 A resolution |
699366 |
| 1.14.20.1 | crystallization of mutant delta R307A, with Fe2+, succinate and CO2, 1.96 A resolution |
699366 |
| 1.14.20.1 | crystallization with 5-hydroxy-4-ketovaleric acid, 1.53 A resolution |
699366 |
