EC Number   |
|---|
    3.5.1.1 | - |
| 3.5.1.1 | atomic resolution structure |
| 3.5.1.1 | comparison between the crystal and solution structures |
| 3.5.1.1 | complexed with the L- and D-stereoisomers of the suicide inhibitor L-6-diazo-5-oxy-norleucine and D-6-diazo-5-oxynorleucine solved using X-ray crystallography and refined with data extending to 1.7 A |
| 3.5.1.1 | crystal structures in complex with L-aspartic acid and with L-glutamic acid. The enzyme conformations open and closed correspond to the inactive and active states, respectively. The binding of ligands induces the positioning of the catalytic Thr15 into its active conformation, which in turn allows for the ordering and closure of the flexible N-terminal loop. L-Aspartic acid is more efficient than L-glutamic acid in inducing the active positioning of Thr15 |
| 3.5.1.1 | crystals are grown by the hanging-drop vapour-diffusion technique at 22°C. The crystal structures of Erwinia carotovora L-asparaginase complexed with L-aspartate and L-glutamate are determined at 1.9 A and 2.2 A, respectively |
| 3.5.1.1 | hanging drop vapor diffusion method, using 0.2 M ammonium sulfate, 0.1 M MES at pH 6.0, and 13-15% (w/v) PEG 3350 |
| 3.5.1.1 | hanging drop vapor diffusion method, using 2.2-2.5 M sodium malonate (pH 7.0) |
| 3.5.1.1 | hanging-drop vapour-diffusion method, X-ray structure of the enzyme, crystallized in a new form, space group C2 and refined to 1.95 A resolution, is compared with that of the previously determined crystal for, space group P2(1) |
| 3.5.1.1 | high-resultion crystal structures of the complex of L-asparaginase with L-Glu, D-Asp and succinic acid |
