8H5P
Crystal Structure of SARS-CoV-2 Main Protease (Mpro) Double Mutant (L50F and E166V) 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 | 45.650, 63.810, 105.761 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 27.900 - 1.670 |
R-factor | 0.1818 |
Rwork | 0.180 |
R-free | 0.20750 |
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] | 27.900 | 27.900 | 1.770 |
High resolution limit [Å] | 1.670 | 4.930 | 1.670 |
Rmerge | 0.059 | 0.028 | 0.681 |
Rmeas | 0.061 | 0.029 | 0.707 |
Total number of observations | 490877 | ||
Number of reflections | 36756 | 1570 | 5779 |
<I/σ(I)> | 25 | 78.03 | 3.51 |
Completeness [%] | 99.7 | 99 | 98.7 |
Redundancy | 13.355 | 12.764 | 13.781 |
CC(1/2) | 1.000 | 0.999 | 0.922 |
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 2 pH 7.5 (sodium HEPES, MOPS acid), 20% v/v ethylene glycol, 10% w/v PEG 8,000 |