7SFI
SARS-CoV-2 Main Protease (Mpro) in Complex with ML104
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL9-2 |
Synchrotron site | SSRL |
Beamline | BL9-2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2021-01-27 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.97946 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 45.490, 63.586, 105.640 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 35.240 - 1.950 |
R-factor | 0.1973 |
Rwork | 0.195 |
R-free | 0.23860 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6lze |
RMSD bond length | 0.008 |
RMSD bond angle | 1.573 |
Data reduction software | XDS |
Data scaling software | SCALA (3.3.22) |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 105.640 | 35.213 | 2.060 |
High resolution limit [Å] | 1.950 | 6.170 | 1.950 |
Rmerge | 0.020 | 0.583 | |
Rmeas | 0.073 | 0.024 | 0.679 |
Rpim | 0.037 | 0.012 | 0.341 |
Total number of observations | 83476 | 2669 | 12310 |
Number of reflections | 22730 | 784 | 3302 |
<I/σ(I)> | 13 | 37.2 | 2.2 |
Completeness [%] | 98.8 | 95.3 | 99.3 |
Redundancy | 3.7 | 3.4 | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 289.15 | Sitting drops consisted of 0.19 uL A:0.19 uL B: A) 5.5 mg/mL Mpro + 0.5 mM ML104 in in 20 mM Tris pH 7.3 + 2 mM DTT + 5 % DMSO B) 0.1 M MES pH 6 + 14 % w/v PEG 4000 Cryoprotectant was 30% v/v glycerol. |