7WQB
SARS-CoV-2 main protease mutant (P168A) in complex with MG-132
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE TPS 05A |
| Synchrotron site | NSRRC |
| Beamline | TPS 05A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2021-03-26 |
| Detector | RAYONIX MX300-HS |
| Wavelength(s) | 1.00000 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 113.977, 53.483, 45.408 |
| Unit cell angles | 90.00, 101.64, 90.00 |
Refinement procedure
| Resolution | 23.430 - 1.870 |
| R-factor | 0.1915 |
| Rwork | 0.188 |
| R-free | 0.22770 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6y2e 6lu7 |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.851 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.19.2_4158) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.940 |
| High resolution limit [Å] | 1.870 | 1.870 |
| Rmerge | 0.044 | 0.297 |
| Number of reflections | 22258 | 2144 |
| <I/σ(I)> | 29.27 | 4.27 |
| Completeness [%] | 99.6 | 96.7 |
| Redundancy | 3.8 | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.1 M MMT (Malic acid, MES, Tris) buffer pH 6.0, 25 % w/v PEG 1500 |
