8HUS
Crystal structure of SARS main protease in complex with S217622
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL02U1 |
| Synchrotron site | SSRF |
| Beamline | BL02U1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2022-08-23 |
| Detector | DECTRIS EIGER X 9M |
| Wavelength(s) | 0.97918 |
| Spacegroup name | P 1 |
| Unit cell lengths | 55.698, 60.855, 68.387 |
| Unit cell angles | 90.21, 102.20, 108.84 |
Refinement procedure
| Resolution | 29.840 - 1.970 |
| R-factor | 0.207077585864 |
| Rwork | 0.206 |
| R-free | 0.23721 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.937 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.12_2829) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 29.840 | 2.070 |
| High resolution limit [Å] | 1.970 | 1.970 |
| Rmerge | 0.026 | 0.039 |
| Number of reflections | 56049 | 8322 |
| <I/σ(I)> | 10.1 | |
| Completeness [%] | 95.2 | |
| Redundancy | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.1 M HEPES pH 7.5, 10% w/v Polyethylene glycol 8,000, 8% v/v Ethylene glycol |
