8SXO
Crystal Structure of SARS-CoV-2 Main Protease (Mpro) H164I 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 | 2022-11-11 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 1.0 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 113.141, 52.905, 45.503 |
Unit cell angles | 90.00, 102.21, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.760 |
R-factor | 0.20584 |
Rwork | 0.201 |
R-free | 0.24361 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.006 |
RMSD bond angle | 0.985 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0352) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.810 |
High resolution limit [Å] | 2.760 | 2.760 |
Rmerge | 0.096 | 0.278 |
Number of reflections | 6368 | 279 |
<I/σ(I)> | 12.21 | 2.24 |
Completeness [%] | 93.0 | 84.3 |
Redundancy | 3.1 |
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 |