8DFE
Crystal Structure of SARS-CoV-2 Main Protease (Mpro) S144L Mutant
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2022-06-04 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1.0 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 113.554, 54.075, 44.615 |
Unit cell angles | 90.00, 100.73, 90.00 |
Refinement procedure
Resolution | 48.710 - 1.890 |
R-factor | 0.2114 |
Rwork | 0.208 |
R-free | 0.26770 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 7lyh |
RMSD bond length | 0.005 |
RMSD bond angle | 1.108 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.920 |
High resolution limit [Å] | 1.890 | 1.890 |
Rmerge | 0.071 | 0.665 |
Number of reflections | 20077 | 988 |
<I/σ(I)> | 26.7 | 2.63 |
Completeness [%] | 94.0 | |
Redundancy | 6.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293.15 | 25% PEG 3350, 0.1M Potassium/Sodium Tartrate, 0.005M Magnesium Chloride |