6M0K
The crystal structure of COVID-19 main protease in complex with an inhibitor 11b
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 | 2020-02-03 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 0.978 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 98.152, 81.701, 51.669 |
Unit cell angles | 90.00, 114.69, 90.00 |
Refinement procedure
Resolution | 43.448 - 1.504 |
R-factor | 0.18 |
Rwork | 0.179 |
R-free | 0.19310 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6lu7 |
RMSD bond length | 0.017 |
RMSD bond angle | 1.510 |
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] | 43.448 | 43.448 | 1.540 |
High resolution limit [Å] | 1.500 | 6.730 | 1.500 |
Rmerge | 0.030 | 0.016 | 0.771 |
Rmeas | 0.036 | 0.019 | 0.940 |
Total number of observations | 385405 | ||
Number of reflections | 58415 | 1286 | 7777 |
<I/σ(I)> | 18.69 | 63.08 | 1.3 |
Completeness [%] | 98.8 | 97.9 | 90.3 |
Redundancy | 3.356 | 3.641 | 2.786 |
CC(1/2) | 1.000 | 0.999 | 0.728 |
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 |