8I2C
E. coli tryptophanyl-tRNA synthetase bound with a chemical fragment at the dimerization interface
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL19U1 |
Synchrotron site | SSRF |
Beamline | BL19U1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2020-11-19 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 0.9785 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 61.725, 80.430, 77.136 |
Unit cell angles | 90.00, 106.05, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.070 |
R-factor | 0.2023 |
Rwork | 0.200 |
R-free | 0.23755 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5v0i |
RMSD bond length | 0.007 |
RMSD bond angle | 1.218 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.130 |
High resolution limit [Å] | 2.070 | 2.070 |
Rmerge | 0.069 | 0.568 |
Rmeas | 0.082 | 0.672 |
Rpim | 0.044 | 0.356 |
Total number of observations | 11908 | |
Number of reflections | 44074 | 3433 |
<I/σ(I)> | 13.5 | 2.3 |
Completeness [%] | 99.5 | |
Redundancy | 3.4 | 3.5 |
CC(1/2) | 0.998 | 0.841 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 290 | 0.16M Ammonium sulfate, 0. M HEPES pH 7.5, 25% PEG 3350 |