4ZLV
Crystal structure of the ornithine aminotransferase from Toxoplasma gondii ME49 in a complex with the Schiff base between PLP and Lys286
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 | 56.481, 61.459, 63.435 |
| Unit cell angles | 100.45, 92.39, 108.32 |
Refinement procedure
| Resolution | 30.000 - 1.800 |
| R-factor | 0.16408 |
| Rwork | 0.162 |
| R-free | 0.20591 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4ngo |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.628 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 |
| Refinement software | REFMAC (5.8.0107) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.830 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.030 | 0.460 |
| Number of reflections | 70729 | |
| <I/σ(I)> | 22.1 | 1.5 |
| Completeness [%] | 96.0 | 87.4 |
| Redundancy | 1.8 | 1.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 294 | 0.2 M AmmSO4, 0.1 M Bis-Tris, 25% PEG3350 |
