7BGP

Crystal structure of MG-132 covalently bound to the main protease (3CLpro/Mpro) of SARS-CoV-2 in absence of DTT.

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	2020-12-16
Detector	DECTRIS PILATUS 6M
Wavelength(s)	1.000
Spacegroup name	P 21 21 21
Unit cell lengths	67.853, 99.779, 103.514
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	45.940 - 1.680
R-factor	0.1719
Rwork	0.170
R-free	0.20100
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	7bb2
RMSD bond length	0.010
RMSD bond angle	1.055
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	PHASER
Refinement software	PHENIX (1.19_4085)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	56.110	1.710
High resolution limit [Å]	1.680	1.680
Rmerge	0.092
Number of reflections	80614	4098
<I/σ(I)>	12.5
Completeness [%]	99.8
Redundancy	6.3
CC(1/2)	0.999	0.604

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	293	0.12M Ethylene glycols (Diethylene glycol; Triethylene glycol; Tetraethylene glycol; Pentaethylene glycol) 0.1M Tris/BICINE pH 8.5, 20% v/v PEG 500 MME; 10 % w/v PEG 20000