8H57

Crystal Structure of SARS-CoV-2 Main Protease (Mpro) A193P Mutant 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	45.399, 63.974, 105.469
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	27.800 - 1.550
R-factor	0.1784
Rwork	0.177
R-free	0.20380
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]	27.800	27.800	1.650
High resolution limit [Å]	1.550	4.610	1.550
Rmerge	0.069	0.034	0.646
Rmeas	0.071	0.036	0.670
Total number of observations	607884
Number of reflections	44743	1883	7054
<I/σ(I)>	22.61	69.32	3.71
Completeness [%]	99.1	98.4	98.4
Redundancy	13.586	12.984	13.944
CC(1/2)	1.000	0.999	0.924

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	EVAPORATION		293	0.05% w/v D-Salicin, 0.05% w/v Esculin hydrate, 0.05% w/v Quinine hemisulfate salt monohydrate, 0.05% w/v Tryptamine, 0.05% w/v Arbutin, 0.1 M Buffer System 2 pH 7.5 (sodium HEPES, MOPS acid), 20% v/v ethylene glycol, 10% w/v PEG 8,000