3CUK
Crystal structure of human D-amino acid oxidase: bound to an inhibitor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2005-02-20 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 187.729, 51.145, 153.294 |
| Unit cell angles | 90.00, 110.45, 90.00 |
Refinement procedure
| Resolution | 42.520 - 2.490 |
| R-factor | 0.24342 |
| Rwork | 0.239 |
| R-free | 0.32850 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ve9 |
| RMSD bond length | 0.028 |
| RMSD bond angle | 2.665 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.590 |
| High resolution limit [Å] | 2.490 | 2.490 |
| Rmerge | 0.097 | 0.558 |
| Number of reflections | 46710 | |
| <I/σ(I)> | 11 | 2 |
| Completeness [%] | 96.8 | 95.4 |
| Redundancy | 2.9 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.8 | 298 | 15% PEG 3350, 0.15M POTASSIUM TRICITR TRIS-HCL, pH 7.80, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
