5E3K
Crystal structure of the ornithine aminotransferase from Toxoplasma gondii ME49 in a complex with (S)-4-amino-5-fluoropentanoic acid
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 | 2015-02-23 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.97913 |
Spacegroup name | P 1 |
Unit cell lengths | 56.328, 61.524, 63.555 |
Unit cell angles | 100.72, 92.96, 108.18 |
Refinement procedure
Resolution | 30.000 - 1.700 |
R-factor | 0.1559 |
Rwork | 0.154 |
R-free | 0.19601 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4nog |
RMSD bond length | 0.016 |
RMSD bond angle | 1.749 |
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 | 0.060 | 0.500 |
Number of reflections | 84366 | |
<I/σ(I)> | 20.9 | 1.9 |
Completeness [%] | 97.3 | 95.7 |
Redundancy | 3 | 2.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 0.2 M AmmSO4, 0.1 M Bis-Tris, 25% PEG3350 |