8INT

Crystal Structure of SARS-CoV-2 Main Protease (Mpro) K90R Mutant

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	DIAMOND BEAMLINE I04
Synchrotron site	Diamond
Beamline	I04
Temperature [K]	100
Detector technology	PIXEL
Collection date	2023-03-04
Detector	DECTRIS EIGER2 X 16M
Wavelength(s)	0.953740
Spacegroup name	C 1 2 1
Unit cell lengths	97.118, 81.021, 51.486
Unit cell angles	90.00, 114.92, 90.00

Refinement procedure

Resolution	29.410 - 1.660
R-factor	0.2015
Rwork	0.200
R-free	0.22420
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.005
RMSD bond angle	0.893
Data reduction software	autoPROC
Data scaling software	XSCALE
Phasing software	PHENIX
Refinement software	PHENIX (V1.20)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	29.410	29.410	1.770
High resolution limit [Å]	1.660	4.930	1.660
Rmerge	0.044	0.025	0.808
Rmeas	0.048	0.027	0.873
Number of reflections	42299	1672	6755
<I/σ(I)>	18.77
Completeness [%]	99.6
Redundancy	6.9
CC(1/2)	1.000	1.000	0.859

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	EVAPORATION		293	0.6%(1% w/v Ampicillin sodium salt, 1% w/v Apramycin sulfate salt, 1% w/v Bacitracin, 1% w/v Dihydrostreptomycin sesquisulfate, 1% w/v Gentamicin sulfate, 1% w/v Spectinomycin dihydrochloride pentahydrate), 0.1M(Tris (base); BICINE)PH8,5, 30%(40% v/v PEG 500* MME; 20 % w/v PEG 20000)