7B3E

Crystal structure of myricetin covalently bound to the main protease (3CLpro/Mpro) of SARS-CoV-2

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	2020-11-24
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.9717
Spacegroup name	P 21 21 21
Unit cell lengths	67.834, 101.104, 103.559
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	49.480 - 1.770
R-factor	0.1728
Rwork	0.171
R-free	0.20380
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	7alh
RMSD bond length	0.008
RMSD bond angle	0.927
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX (1.18.2_3874)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	103.560	1.810
High resolution limit [Å]	1.770	1.770
Rmerge	0.110
Number of reflections	70132	3958
<I/σ(I)>	11.3	1.5
Completeness [%]	100.0
Redundancy	8.8
CC(1/2)	0.998	0.570

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