8DPR
Crystal structure of SARS-CoV-2 main protease in complex with inhibitor TKB-248
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL41XU |
Synchrotron site | SPring-8 |
Beamline | BL41XU |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2021-10-09 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 115.403, 53.926, 45.678 |
Unit cell angles | 90.00, 101.63, 90.00 |
Refinement procedure
Resolution | 56.520 - 2.000 |
R-factor | 0.19252 |
Rwork | 0.190 |
R-free | 0.24722 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 7jkv |
RMSD bond length | 0.010 |
RMSD bond angle | 1.648 |
Data reduction software | xia2 |
Data scaling software | DIALS |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0352) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 56.520 | 2.040 |
High resolution limit [Å] | 2.000 | 2.000 |
Number of reflections | 18600 | 888 |
<I/σ(I)> | 9.16 | |
Completeness [%] | 99.9 | |
Redundancy | 8.6 | |
CC(1/2) | 0.997 | 0.672 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 298 | 0.1 M MES, pH 5.8, 15% PEG6000, 3% DMSO |