8P57
Crystal structure of the main protease (3CLpro/Mpro) of SARS-CoV-2 obtained in presence of 75 micromolar X77.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ELETTRA BEAMLINE 11.2C |
Synchrotron site | ELETTRA |
Beamline | 11.2C |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2021-05-12 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.9999 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 67.660, 100.829, 104.647 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 49.500 - 1.600 |
R-factor | 0.1683 |
Rwork | 0.168 |
R-free | 0.18330 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 7bb2 |
RMSD bond length | 0.009 |
RMSD bond angle | 1.124 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX (1.19.2_4158) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 104.650 | 1.630 |
High resolution limit [Å] | 1.600 | 1.600 |
Rmerge | 0.124 | |
Number of reflections | 95019 | 4606 |
<I/σ(I)> | 9.8 | |
Completeness [%] | 100.0 | |
Redundancy | 8.8 | |
CC(1/2) | 0.997 | 0.581 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.1M DL-Glutamic acid monohydrate, 0.1M DL-Alanine 0.1M Glycine 0.1M DL-Lysine monohydrochloride 0.1M DL-Serine, 0.1M Hepes/MOPS pH 7.5, 20% v/v Ethylene glycol 10 % w/v PEG 8000 |