5EAV
Unliganded structure of the ornithine aminotransferase from Toxoplasma gondii
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 | CCD |
| Collection date | 2015-04-06 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 1 |
| Unit cell lengths | 56.338, 61.067, 63.597 |
| Unit cell angles | 100.88, 92.23, 108.14 |
Refinement procedure
| Resolution | 30.000 - 1.600 |
| R-factor | 0.178 |
| Rwork | 0.177 |
| R-free | 0.21400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4nog |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.746 |
| 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 | 1.630 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.067 | 0.460 |
| Number of reflections | 97272 | |
| <I/σ(I)> | 32.1 | 2.86 |
| Completeness [%] | 93.9 | 92.5 |
| Redundancy | 3.6 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 290 | 0.2 M AmmSO4, 0.1 M Bis-Tris, 25% PEG3350, 0.5 mM oxidized glutathione |
