EC Number   |
Reference |
|---|
   3.5.1.77 | hanging drop vapor-diffusion method. Crystal structure of mutant enzymes C172A, C172S, R175A, N173A and the complexes of mutant enzymes R175A and N173A with the substrate N-carbamoyl-D-p-hydroxyphenylglycine |
656143 |
| 3.5.1.77 | hanging drop vapour diffusion method using protein solutions containing 15 mg/ml protein with precipitating solution at room temperature. A222C and A302C mutants are initially grown as micro-crystals with the precipitating condition of 1.2 M lithium sulfate and 0.1 M Hepes buffer (pH 7.0). A micro-seeding method is then applied to obtain large single crystals. For P95C/F304C and P178C, no crystals are obtained. Crystals structures of D-NCase mutants, A302C and A222C |
669884 |
| 3.5.1.77 | hanging-drop vapor-diffusion method, crystals belong to space group P2(1) with unit cell dimensions a = 70.23 A, b = 67.53 A, c = 137.48 A and beta = 96.12°. There are 4 molecules per asymmetric unit |
656486 |
| 3.5.1.77 | hanging-drop vapour diffusion method using lithium sulfate as precipitant. It crystallizes in space group P2(1) with unit-cell parameters a = 69.8 A, b = 67.9 A and c = 137.8 A and beta = 96.4°. There are 4 molecules per asymmetric unit |
654121 |
| 3.5.1.77 | sitting-drop vapour-diffusion method. Native crystals belong to space group P2(1)2(1)2 with a = 67.84 A, b = 137.83 A, c = 68.39 A. Structure determined to 1.7 A resolution. The enzyme forms a homotetramer and each monomer consists of a variant of the alpha + beta fold. The topology of the enzyme comprises a sandwich of parallel beta sheets surrounded by two layers of alpha helices |
657376 |
