9EYA
Complex of a mutant of the SARS-CoV-2 main protease Mpro with the nsp4/5 substrate peptide (soaking).
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2022-06-04 |
| Detector | DECTRIS EIGER2 X 16M |
| Wavelength(s) | 0.8856 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 113.694, 52.191, 45.154 |
| Unit cell angles | 90.00, 103.31, 90.00 |
Refinement procedure
| Resolution | 47.200 - 1.700 |
| R-factor | 0.16 |
| Rwork | 0.159 |
| R-free | 0.18550 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.721 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.200 | 1.730 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.068 | 1.103 |
| Rmeas | 0.075 | 1.278 |
| Rpim | 0.031 | 0.633 |
| Number of reflections | 26488 | 911 |
| <I/σ(I)> | 11.9 | 1.1 |
| Completeness [%] | 93.3 | |
| Redundancy | 5.5 | |
| CC(1/2) | 0.998 | 0.487 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 291 | 0.1 M MMT (DL-malic acid, MES, and Tris base in molar ratio 1:2:2), pH 7.0, 25% PEG 1500 |
