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 |