8P58

Crystal structure of the main protease (3CLpro/Mpro) of SARS-CoV-2 obtained in presence of 500 micromolar X77 enantiomer R.

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	2021-06-02
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.9718
Spacegroup name	P 21 21 21
Unit cell lengths	67.688, 100.828, 104.329
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	49.480 - 1.550
R-factor	0.1599
Rwork	0.159
R-free	0.17900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	7bb2
RMSD bond length	0.012
RMSD bond angle	1.183
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX (1.19.2_4158)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	104.330	1.580
High resolution limit [Å]	1.550	1.550
Rmerge	0.107
Number of reflections	104143	5143
<I/σ(I)>	12.5
Completeness [%]	100.0
Redundancy	10.8
CC(1/2)	0.999	0.653

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	0.12M 1,6-Hexanediol 0.12M 1-Butanol 0.12M 1,2-Propanediol 0.12M 2-Propanol 0.12M 1,4-Butanediol 0.12M 1,3-Propanediol, 0.1 M Tris/Bicine pH 8.5, 20% v/v Ethylene glycol 10% w/v PEG 8000