EC Number   |
|---|
    1.4.1.1 | - |
| 1.4.1.1 | crystal structure of the NAD-bound enzyme at 2.3 A in a C2 crystal form with the 70000 Da dimer in the asymmetric unit |
| 1.4.1.1 | hanging drop vapour diffusion method, crystals of apo-AlaDH are grown using 0.4 M ammonium hydrogenphosphate as reservoir solution at 20°C |
| 1.4.1.1 | hanging-drop method |
| 1.4.1.1 | hanging-drop vapour diffusion method. Crystallized in several forms. One polymorph growing in space group P2(1)2(1)2(1) has non-crystallographic symmetry that becomes crystallographic, changing the space group to P2(1)2(1)2(1) upon binding iridium or samarium |
| 1.4.1.1 | identificaion of putative inhibitors by molecular docking |
| 1.4.1.1 | investigation of functional domain motions by using the Gaussian network model and the anisotropy network model. The domain motions have a common hinge axis centered in residues Met133 and Met301. Both the NAD-binding domain and the substrate-binding domain move in a highly coupled way. The first three slowest modes exhibit the open-closed, rotation and twist motions |
| 1.4.1.1 | purified recombinant His6-tagged enzyme, hanging drop vapour diffusion method, 15 mg/ml protein in 20 mM Tris-HCl, pH 8.0, mixed with 0.1 M HEPES, pH 8.0, 12% w/v PEG 8000, and 8% v/v ethylene glycol, 4°C, method optimization, X-ray diffraction structure determination and analysis at 2.35 A resolution |
| 1.4.1.1 | structure of the NAD+-bound AF1665 AlaDH at 2.3 A in a C2 crystal form with the 70000 Da dimer as the asymmetric unit |
| 1.4.1.1 | to 2.8 A resoution, triclinic space group P1 |
