9L13
The crystal structure of SARS-CoV-2 Main protease in complex with an iso-quinoline-derived inhibitor FD6-31
This is a non-PDB format compatible entry.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL10U2 |
| Synchrotron site | SSRF |
| Beamline | BL10U2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2024-06-18 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.97918 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 97.150, 80.900, 51.550 |
| Unit cell angles | 90.00, 114.67, 90.00 |
Refinement procedure
| Resolution | 44.140 - 1.960 |
| R-factor | 0.1994 |
| Rwork | 0.198 |
| R-free | 0.23270 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 7vic |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.357 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | MOLREP |
| Refinement software | PHENIX ((1.19.2_4158: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 59.640 | 2.040 |
| High resolution limit [Å] | 1.960 | 1.960 |
| Number of reflections | 25791 | 295 |
| <I/σ(I)> | 20 | |
| Completeness [%] | 98.7 | |
| Redundancy | 2 | |
| CC(1/2) | 0.990 | 0.990 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 289.15 | 0.1 M Bis-Tris 6.5, 20% PEG5000MME |
