6LZE
The crystal structure of COVID-19 main protease in complex with an inhibitor 11a
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NFPSS BEAMLINE BL19U1 |
Synchrotron site | NFPSS |
Beamline | BL19U1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2020-02-02 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 0.978 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 97.696, 80.938, 51.738 |
Unit cell angles | 90.00, 114.27, 90.00 |
Refinement procedure
Resolution | 47.165 - 1.505 |
R-factor | 0.1768 |
Rwork | 0.176 |
R-free | 0.19890 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6lu7 |
RMSD bond length | 0.014 |
RMSD bond angle | 1.327 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (1.12_2829) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 47.165 | 47.165 | 1.540 |
High resolution limit [Å] | 1.500 | 6.730 | 1.510 |
Rmerge | 0.042 | 0.028 | 0.555 |
Rmeas | 0.050 | 0.033 | 0.677 |
Number of reflections | 57378 | 1273 | 6991 |
<I/σ(I)> | 13.99 | 36.7 | 1.8 |
Completeness [%] | 98.0 | 97.8 | 82.2 |
Redundancy | 3.287 | 3.578 | 2.746 |
CC(1/2) | 0.999 | 0.998 | 0.785 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | EVAPORATION | 6 | 293 | 2% polyethylene glycol (PEG) 6000, 3% DMSO, 1mM DTT, 0.1M MES buffer (pH 6.0), protein concentration 5mg/ml, VAPOR DIFFUSION, HANGING DROP, temperature 293K |