7MLG
Crystal Structure of SARS-CoV-2 Main Protease (3CLpro/Mpro) Covalently Bound to Compound C63
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-C |
Synchrotron site | APS |
Beamline | 24-ID-C |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2021-04-04 |
Detector | DECTRIS EIGER2 X 16M |
Wavelength(s) | 0.97918 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 113.450, 53.318, 45.474 |
Unit cell angles | 90.00, 101.88, 90.00 |
Refinement procedure
Resolution | 48.110 - 2.500 |
R-factor | 0.22899 |
Rwork | 0.224 |
R-free | 0.26800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6y2e |
RMSD bond length | 0.005 |
RMSD bond angle | 1.237 |
Data reduction software | DIALS |
Data scaling software | DIALS |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.110 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Number of reflections | 9329 | 1710 |
<I/σ(I)> | 12.52 | 1.3 |
Completeness [%] | 97.9 | 99.1 |
Redundancy | 2.8 | |
CC(1/2) | 0.998 | 0.786 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 295 | 0.1 M BTP, pH 6.5, 20% PEG3350, 0.2 M potassium thiocyanate |