4A0G
Structure of bifunctional DAPA aminotransferase-DTB synthetase from Arabidopsis thaliana in its apo form.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM30A |
| Synchrotron site | ESRF |
| Beamline | BM30A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-10-30 |
| Detector | ADSC QUANTUM 315r |
| Spacegroup name | P 1 |
| Unit cell lengths | 79.442, 80.066, 136.939 |
| Unit cell angles | 99.96, 107.12, 97.25 |
Refinement procedure
| Resolution | 39.574 - 2.502 |
| R-factor | 0.1803 |
| Rwork | 0.177 |
| R-free | 0.23910 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4a0f |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.325 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.140 | 2.550 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.050 | 0.420 |
| Number of reflections | 95045 | |
| <I/σ(I)> | 14.81 | 1.91 |
| Completeness [%] | 88.0 | 48.3 |
| Redundancy | 1.95 | 1.92 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | BISTRIS 0.1 M PH 5.9, 0.2 M LISO4, 15 % PEG3350 |
