8H3K

Crystal Structure of SARS-CoV-2 Main Protease (Mpro) Double Mutant (L50F and E166V) in Complex with Inhibitor Enstrelvir

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRF BEAMLINE BL02U1
Synchrotron site	SSRF
Beamline	BL02U1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2022-08-17
Detector	DECTRIS EIGER2 S 9M
Wavelength(s)	0.978642
Spacegroup name	P 1 21 1
Unit cell lengths	55.543, 98.875, 58.991
Unit cell angles	90.00, 108.00, 90.00

Refinement procedure

Resolution	52.830 - 1.800
R-factor	0.1693
Rwork	0.168
R-free	0.20130
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	7vu6
Data scaling software	XDS (2020-12-02)
Phasing software	PHENIX (1.20.1_4487)
Refinement software	PHENIX (1.20.1_4487)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	52.830	52.830	1.910
High resolution limit [Å]	1.800	5.380	1.800
Rmerge	0.079	0.034	0.788
Rmeas	0.085	0.037	0.854
Total number of observations	377786
Number of reflections	54655	2134	8666
<I/σ(I)>	15.29	46.92	2.35
Completeness [%]	97.4	98.2	95.8
Redundancy	6.912	7.109	6.451
CC(1/2)	0.999	0.999	0.833

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		293.15	0.3% w/v Sodium-L ascorbate, 0.3% w/v Choline Chloride, 0.3% v/v D-Panthenol, 0.3% w/v Pyridoxine hydrochloride, 0.3% w/v Thiamine hydrochloride 20% v/v PEG 500* MME; 10% w/v PEG 20000; 0.1 M 0.1 M Buffer System 2 pH 7.5 (sodium HEPES, MOPS acid)