5E3K
Crystal structure of the ornithine aminotransferase from Toxoplasma gondii ME49 in a complex with (S)-4-amino-5-fluoropentanoic acid
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-D |
| Synchrotron site | APS |
| Beamline | 21-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-02-23 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97913 |
| Spacegroup name | P 1 |
| Unit cell lengths | 56.328, 61.524, 63.555 |
| Unit cell angles | 100.72, 92.96, 108.18 |
Refinement procedure
| Resolution | 30.000 - 1.700 |
| R-factor | 0.1559 |
| Rwork | 0.154 |
| R-free | 0.19601 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4nog |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.749 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0124) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.730 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.060 | 0.500 |
| Number of reflections | 84366 | |
| <I/σ(I)> | 20.9 | 1.9 |
| Completeness [%] | 97.3 | 95.7 |
| Redundancy | 3 | 2.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 0.2 M AmmSO4, 0.1 M Bis-Tris, 25% PEG3350 |
