7N8C
Joint X-ray/neutron structure of SARS-CoV-2 main protease (Mpro) in complex with Mcule5948770040
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 293 |
Detector technology | PIXEL |
Collection date | 2021-03-10 |
Detector | DECTRIS EIGER R 4M |
Wavelength(s) | 1.54 |
Spacegroup name | I 1 2 1 |
Unit cell lengths | 55.314, 81.301, 88.578 |
Unit cell angles | 90.00, 96.46, 90.00 |
Refinement procedure
Resolution | 12.860 - 2.500 |
Rwork | 0.187 |
R-free | 0.21100 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 1.100 |
Data reduction software | CrysalisPro |
Data scaling software | CrysalisPro |
Phasing software | PHASER |
Refinement software | nCNS (1.0.0) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 59.720 | 2.590 | 2.270 |
High resolution limit [Å] | 2.200 | 2.500 | 2.200 |
Rmerge | 0.107 | 0.283 | 0.602 |
Rpim | 0.055 | ||
Number of reflections | 19108 | 1176 | 1884 |
<I/σ(I)> | 11.4 | 5.8 | 1.6 |
Completeness [%] | 96.3 | 88.4 | 94.7 |
Redundancy | 4.7 | 5.6 | 4.8 |
CC(1/2) | 0.992 | 0.686 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 293 | 18% PEG3350, 0.1 M Bis-Tris pH 7.0 reservoir solution and 0.2 microL microseeds at 1:200 dilution |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 293 | 18% PEG3350, 0.1 M Bis-Tris pH 7.0 reservoir solution and 0.2 microL microseeds at 1:200 dilution |