4ZWM
2.3 A resolution crystal structure of the ornithine aminotransferase from Toxoplasma gondii ME49
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 | 2015-03-23 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.9788 |
| Spacegroup name | P 1 |
| Unit cell lengths | 56.418, 60.804, 63.379 |
| Unit cell angles | 100.70, 92.63, 107.68 |
Refinement procedure
| Resolution | 30.000 - 2.310 |
| R-factor | 0.1899 |
| Rwork | 0.186 |
| R-free | 0.25848 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4nog |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.561 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0107) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.340 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.070 | 0.490 |
| Number of reflections | 33287 | |
| <I/σ(I)> | 15.7 | 2.2 |
| Completeness [%] | 96.9 | 97.2 |
| Redundancy | 2 | 1.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 293 | 0.2 M AmmSO4, 0.1 M Bis-Tris, 25% PEG3350 |
