5EQC
Structure of the ornithine aminotransferase from Toxoplasma gondii crystallized in presence of oxidized glutathione reveals partial occupancy of PLP at the protein active site
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 | 2015-04-13 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 43 |
| Unit cell lengths | 109.406, 109.406, 109.883 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.200 |
| R-factor | 0.146 |
| Rwork | 0.145 |
| R-free | 0.18100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4nog |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.915 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0131) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.240 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.110 | 0.700 |
| Number of reflections | 65316 | |
| <I/σ(I)> | 23.4 | 3.3 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 8.3 | 8.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.2 M Na Thiocyanate, 20% PEG3350, 0.5 mM oxidized glutathione |
