2EFX
The crystal structure of D-amino acid amidase from Ochrobactrum anthropi SV3 complexed with L-phenylalanine amide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL41XU |
| Synchrotron site | SPring-8 |
| Beamline | BL41XU |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-11-11 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 76.711, 123.396, 115.477 |
| Unit cell angles | 90.00, 104.36, 90.00 |
Refinement procedure
| Resolution | 19.820 - 2.200 |
| R-factor | 0.19035 |
| Rwork | 0.187 |
| R-free | 0.25613 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | DAA native structure (2DRW) |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.356 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.280 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.072 | 0.265 |
| Number of reflections | 103243 | |
| Completeness [%] | 98.1 | 85.6 |
| Redundancy | 4.7 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 |
