9ARS
Crystal structure of SARS-CoV-2 main protease E166V mutant in complex with an inhibitor TKB-245
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS-II BEAMLINE 19-ID |
Synchrotron site | NSLS-II |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2023-09-17 |
Detector | DECTRIS EIGER X 4M |
Wavelength(s) | 0.979497 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 45.931, 53.951, 114.966 |
Unit cell angles | 90.00, 100.38, 90.00 |
Refinement procedure
Resolution | 48.690 - 2.400 |
R-factor | 0.17991 |
Rwork | 0.178 |
R-free | 0.22195 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 1.690 |
Data reduction software | xia2 |
Data scaling software | DIALS |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0425) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 45.180 | 2.510 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.066 | 0.524 |
Number of reflections | 21740 | 2641 |
<I/σ(I)> | 14.26 | |
Completeness [%] | 98.7 | |
Redundancy | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 298 | 0.1 M HEPES pH 7.5, 14 % w/v Polyethylene glycol 3,350 |