4M0J
Crystal structure of a D-amino acid aminotransferase from Burkholderia thailandensis E264
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2013-07-17 |
| Detector | MAR scanner 300 mm plate |
| Wavelength(s) | 0.9798 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 115.600, 73.980, 76.210 |
| Unit cell angles | 90.00, 105.35, 90.00 |
Refinement procedure
| Resolution | 44.190 - 2.050 |
| R-factor | 0.18141 |
| Rwork | 0.179 |
| R-free | 0.22374 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1daa |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.527 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.100 |
| High resolution limit [Å] | 2.050 | 2.050 |
| Rmerge | 0.045 | 0.443 |
| Number of reflections | 39005 | |
| <I/σ(I)> | 19.8 | 3.18 |
| Completeness [%] | 99.6 | 100 |
| Redundancy | 3.74 | 3.76 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 289 | 25% PEG4000, 0.2M Cacl2, 0.1M Tris pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
