5VAD
Crystal structure of human Prolyl-tRNA synthetase (PRS) in complex with inhibitor
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 5.0.3 |
Synchrotron site | ALS |
Beamline | 5.0.3 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-10-01 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.98 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 71.089, 92.278, 84.832 |
Unit cell angles | 90.00, 111.18, 90.00 |
Refinement procedure
Resolution | 19.930 - 2.360 |
R-factor | 0.1991 |
Rwork | 0.196 |
R-free | 0.26160 |
RMSD bond length | 0.012 |
RMSD bond angle | 1.549 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.410 |
High resolution limit [Å] | 2.360 | 6.430 | 2.370 |
Rmerge | 0.071 | 0.047 | 0.660 |
Number of reflections | 41903 | ||
<I/σ(I)> | 11.4 | ||
Completeness [%] | 99.8 | 99.5 | 97 |
Redundancy | 3.7 | 3.6 | 2.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 20% PEG3350, 500mM CaCl2, Hepes pH7.5 |