8H5F
Crystal Structure of SARS-CoV-2 Main Protease (Mpro) L167F Mutant in Complex with Inhibitor Nirmatrelvir
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I04 |
Synchrotron site | Diamond |
Beamline | I04 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2022-08-10 |
Detector | DECTRIS EIGER2 X 16M |
Wavelength(s) | 0.953740 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 45.373, 63.825, 105.839 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 27.330 - 1.790 |
R-factor | 0.1869 |
Rwork | 0.184 |
R-free | 0.22730 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 7vh8 |
RMSD bond length | 0.008 |
RMSD bond angle | 1.046 |
Data reduction software | autoPROC |
Data scaling software | XSCALE |
Phasing software | PHENIX |
Refinement software | PHENIX (1.19.2_4158) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 27.330 | 27.330 | 1.900 |
High resolution limit [Å] | 1.790 | 5.280 | 1.790 |
Rmerge | 0.080 | 0.033 | 0.658 |
Rmeas | 0.083 | 0.035 | 0.684 |
Number of reflections | 29844 | 1288 | 4729 |
<I/σ(I)> | 21.05 | ||
Completeness [%] | 99.9 | ||
Redundancy | 13.3 | ||
CC(1/2) | 1.000 | 0.999 | 0.919 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | EVAPORATION | 293 | 0.2% w/v Lidocaine hydrochloride monohydrate, 0.2% w/v Procaine hydrochloride, 0.2% w/v Proparacaine hydrochloride, 0.2% w/v tetracaine hydrochloride, 0.1 M Buffer System 3 pH 8.5 (Tris base, BICINE), 20% v/v ethylene glycol, 10% w/v PEG 8,000 |