8H4Y
Crystal Structure of SARS-CoV-2 Main Protease (Mpro) F140L 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 | 45.965, 64.457, 105.116 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 27.870 - 2.250 |
R-factor | 0.21 |
Rwork | 0.206 |
R-free | 0.24760 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 7vh8 |
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] | 27.870 | 27.870 | 2.380 |
High resolution limit [Å] | 2.250 | 6.580 | 2.250 |
Rmerge | 0.086 | 0.042 | 0.797 |
Rmeas | 0.090 | 0.044 | 0.829 |
Total number of observations | 201282 | ||
Number of reflections | 15428 | 684 | 2420 |
<I/σ(I)> | 18.95 | 48.6 | 3.3 |
Completeness [%] | 99.6 | 96.9 | 99.1 |
Redundancy | 13.047 | 12 | 13.187 |
CC(1/2) | 0.999 | 0.999 | 0.880 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | EVAPORATION | 293 | 0.05% w/v (-)-Menthol, 0.05% w/v Caffeic acid, 0.05% w/v D-Quinic acid, 0.05% w/v Shikimic acid, 0.05% w/v Gallic acidmonohydrate, 0.05% w/v N-Vanillylnonanamide, 0.05% w/v Thymol, 0.1 M Buffer System 2 pH 7.5 (sodium HEPES, MOPS acid), 20% v/v ethylene glycol, 10% w/v PEG 8,000 |