4A0H
Structure of bifunctional DAPA aminotransferase-DTB synthetase from Arabidopsis thaliana bound to 7-keto 8-amino pelargonic acid (KAPA)
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 |
| Detector | ADSC QUANTUM 315r |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 235.320, 76.940, 89.220 |
| Unit cell angles | 90.00, 109.89, 90.00 |
Refinement procedure
| Resolution | 44.572 - 2.808 |
| R-factor | 0.197 |
| Rwork | 0.193 |
| R-free | 0.26190 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4a0f |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.354 |
| 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] | 44.570 | 2.880 |
| High resolution limit [Å] | 2.810 | 2.810 |
| Rmerge | 0.110 | 0.650 |
| Number of reflections | 36581 | |
| <I/σ(I)> | 9.22 | 1.61 |
| Completeness [%] | 99.0 | 91.5 |
| Redundancy | 3.78 | 1.74 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 0.2 M AMMONIUM TARTRATE PH 6.2, 15 % PEG3350 |
