5E5I
Structure of the ornithine aminotransferase from Toxoplasma gondii in complex with inactivator
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) | 0.97889 |
| Spacegroup name | P 1 |
| Unit cell lengths | 56.408, 61.445, 63.665 |
| Unit cell angles | 100.87, 92.48, 108.12 |
Refinement procedure
| Resolution | 30.000 - 1.700 |
| R-factor | 0.17054 |
| Rwork | 0.168 |
| R-free | 0.20784 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4nog |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.844 |
| 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 | 0.054 | 0.670 |
| Number of reflections | 81340 | |
| <I/σ(I)> | 35.4 | 2.06 |
| Completeness [%] | 92.6 | 95.6 |
| Redundancy | 3.8 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 291 | 0.2 M AmmSO4, 0.1 M Bis-Tris, 25% PEG3350 |
