23LX
Crystal structure of SARS-CoV-2 main protease P168 deletion mutant in complex with leritrelvir
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 | 2024-09-08 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.97923 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 114.267, 53.048, 46.225 |
| Unit cell angles | 90.00, 102.74, 90.00 |
Refinement procedure
| Resolution | 55.728 - 1.700 |
| Rwork | 0.178 |
| R-free | 0.23050 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.522 |
| Data reduction software | XDS (BUILT 20240630) |
| Data scaling software | Aimless (0.7.7) |
| Phasing software | PHASER (2.8.3) |
| Refinement software | REFMAC (5.8.0430) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 55.730 | 1.730 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.115 | 0.848 |
| Number of reflections | 29555 | 1351 |
| <I/σ(I)> | 12.8 | 2.1 |
| Completeness [%] | 99.1 | |
| Redundancy | 6.3 | |
| CC(1/2) | 0.998 | 0.513 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 289 | 0.1 M Sodium citrate tribasic dihydrate pH 5.5, 16% w/v Polyethylene glycol 8,000 |
