9ZNL
X-ray structure of SARS-CoV-2 main protease covalently bound to inhibitor GRL-050-22 at 1.16 A
This is a non-PDB format compatible entry.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2022-12-13 |
| Detector | DECTRIS EIGER2 X 16M |
| Wavelength(s) | 0.97872 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 97.950, 82.339, 54.291 |
| Unit cell angles | 90.00, 117.44, 90.00 |
Refinement procedure
| Resolution | 20.290 - 1.160 |
| R-factor | 0.1414 |
| Rwork | 0.141 |
| R-free | 0.15940 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.206 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX (1.21.2_5419) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.290 | 1.190 |
| High resolution limit [Å] | 1.160 | 1.160 |
| Rmerge | 0.068 | |
| Number of reflections | 245345 | 16802 |
| <I/σ(I)> | 8.03 | 1.05 |
| Completeness [%] | 95.9 | 94.77 |
| Redundancy | 2 | |
| CC(1/2) | 0.995 | 0.594 |
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 |
