8U4Y
Crystal Structure of SARS-CoV-2 Main Protease (Mpro) L50F Mutant
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2022-09-22 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 0.97918 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 48.228, 105.474, 53.792 |
Unit cell angles | 90.00, 104.50, 90.00 |
Refinement procedure
Resolution | 46.740 - 2.210 |
R-factor | 0.18191 |
Rwork | 0.179 |
R-free | 0.23876 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.005 |
RMSD bond angle | 1.418 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0419) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.260 |
High resolution limit [Å] | 2.210 | 2.220 |
Rmerge | 0.133 | 0.517 |
Number of reflections | 25847 | 1265 |
<I/σ(I)> | 17.3 | 2.41 |
Completeness [%] | 99.4 | |
Redundancy | 6.2 | 4.4 |
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 |