9VUV
Crystal structure of SADS-CoV main protease (Lys35Val/Cys224Ser) in complex with SY110
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 | 2024-09-26 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.97853 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 90.827, 184.746, 63.802 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 31.440 - 2.000 |
| R-factor | 0.1883 |
| Rwork | 0.187 |
| R-free | 0.21810 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.907 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((1.18.2_3874: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 34.590 | 2.040 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.125 | 1.616 |
| Rmeas | 0.130 | 1.685 |
| Rpim | 0.036 | 0.470 |
| Number of reflections | 73454 | 4446 |
| <I/σ(I)> | 17.8 | 2 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 13 | 12.5 |
| CC(1/2) | 0.999 | 0.675 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6 | 291 | 0.1 M PCTP pH 6.0, 25% w/v PEG 1500 |
