7DAV
The native crystal structure of COVID-19 main protease
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL19U1 |
Synchrotron site | SSRF |
Beamline | BL19U1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2020-06-03 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.98 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 113.941, 53.795, 44.716 |
Unit cell angles | 90.00, 101.53, 90.00 |
Refinement procedure
Resolution | 50.000 - 1.770 |
R-factor | 0.2085 |
Rwork | 0.206 |
R-free | 0.24750 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6lu7 |
RMSD bond length | 0.008 |
RMSD bond angle | 0.997 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | PHASER |
Refinement software | REFMAC (2.2.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.800 |
High resolution limit [Å] | 1.770 | 1.770 |
Rmerge | 0.070 | 0.542 |
Number of reflections | 25744 | 1251 |
<I/σ(I)> | 24.3 | 2.4 |
Completeness [%] | 99.3 | |
Redundancy | 6.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 295 | 200mM KF and 15% PEG 3350 |