8H5P

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

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	2022-08-10
Detector	DECTRIS EIGER2 X 16M
Wavelength(s)	0.953740
Spacegroup name	P 21 21 2
Unit cell lengths	45.650, 63.810, 105.761
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	27.900 - 1.670
R-factor	0.1818
Rwork	0.180
R-free	0.20750
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	7vh8
Data reduction software	autoPROC
Data scaling software	XSCALE
Phasing software	PHENIX
Refinement software	PHENIX (1.19.2_4158)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	27.900	27.900	1.770
High resolution limit [Å]	1.670	4.930	1.670
Rmerge	0.059	0.028	0.681
Rmeas	0.061	0.029	0.707
Total number of observations	490877
Number of reflections	36756	1570	5779
<I/σ(I)>	25	78.03	3.51
Completeness [%]	99.7	99	98.7
Redundancy	13.355	12.764	13.781
CC(1/2)	1.000	0.999	0.922

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	EVAPORATION		293	0.2% w/v Lidocaine hydrochloride monohydrate, 0.2% w/v Procaine hydrochloride, 0.2% w/v Proparacaine hydrochloride, 0.2% w/v tetracaine hydrochloride, 0.1 M Buffer System 2 pH 7.5 (sodium HEPES, MOPS acid), 20% v/v ethylene glycol, 10% w/v PEG 8,000