9E8R
X-ray structure of SARS-CoV-2 main protease T190I covalently bound to compound GRL-051-22 at 1.5 A
This is a non-PDB format compatible entry.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU MICROMAX-007 HF |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2024-09-20 |
| Detector | DECTRIS EIGER2 S 4M |
| Wavelength(s) | 1.5406 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 97.753, 82.116, 54.209 |
| Unit cell angles | 90.00, 117.40, 90.00 |
Refinement procedure
| Resolution | 20.530 - 1.500 |
| R-factor | 0.1303 |
| Rwork | 0.129 |
| R-free | 0.16460 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.026 |
| Data reduction software | CrysalisPro |
| Data scaling software | CrysalisPro |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.21.1_5286) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.530 | 1.540 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.050 | 0.701 |
| Rmeas | 0.055 | 0.828 |
| Rpim | 0.023 | 0.429 |
| Number of reflections | 60617 | 4306 |
| <I/σ(I)> | 16.62 | 1.41 |
| Completeness [%] | 99.8 | 99.58 |
| Redundancy | 4.9 | 3.4 |
| CC(1/2) | 0.999 | 0.722 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 277 | 12% PEG 10K, 0.003 M DTT, 1% MPD, 0.05 M MES (pH 6.0), 0.12 M KCl, 2.5% DMSO, 25 mM HEPES, protein concentration 5.5 mg/mL |
