6W63
Structure of COVID-19 main protease bound to potent broad-spectrum non-covalent inhibitor X77
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-G |
Synchrotron site | APS |
Beamline | 21-ID-G |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2020-02-15 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.978 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 45.050, 63.840, 106.588 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.910 - 2.100 |
R-factor | 0.1571 |
Rwork | 0.150 |
R-free | 0.22140 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6lu7 |
RMSD bond length | 0.011 |
RMSD bond angle | 1.094 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX |
Refinement software | PHENIX (1.13_2998) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 | 2.140 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmeas | 0.176 | |
Rpim | 0.061 | 0.237 |
Number of reflections | 18549 | 870 |
<I/σ(I)> | 17.2 | 2.2 |
Completeness [%] | 99.3 | 94 |
Redundancy | 8.5 | 5.7 |
CC(1/2) | 0.986 | 0.797 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 294 | 3 mM DTT, 1% MPD, 80mM KCl, 50 mM MES pH 6.0, 16% PEG 10k 2uL protein ( 125 uM 3CLpro, 25 mM HEPES pH 7.5, 2.5 mM DTT, 1% DMSO, 400 uM 077) + 1 uL reservoir |