5XII
Crystal Structure of Toxoplasma gondii Prolyl-tRNA Synthetase (TgPRS) in complex with inhibitor 6
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-03-23 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.9797 |
| Spacegroup name | P 1 |
| Unit cell lengths | 76.600, 90.730, 92.996 |
| Unit cell angles | 89.94, 99.37, 104.31 |
Refinement procedure
| Resolution | 40.290 - 2.170 |
| R-factor | 0.1773 |
| Rwork | 0.175 |
| R-free | 0.22390 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4twa |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.547 |
| Data reduction software | MxCuBE |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.210 |
| High resolution limit [Å] | 2.170 | 5.890 | 2.170 |
| Rmerge | 0.041 | 0.011 | 0.479 |
| Rmeas | 0.052 | 0.013 | 0.612 |
| Rpim | 0.031 | 0.008 | 0.376 |
| Total number of observations | 337845 | ||
| Number of reflections | 123090 | 5878 | |
| <I/σ(I)> | 11 | ||
| Completeness [%] | 98.1 | 99.3 | 93.5 |
| Redundancy | 2.7 | 2.7 | 2.6 |
| CC(1/2) | 0.999 | 0.703 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 10%(w/v) PEG 8K, 20%(v/v) ethylene glycol, 0.03M of each divalent cation and 0.1M MOPS/HEPES-Na |
