7PFM

A SARS-CoV2 major protease non-covalent ligand structure determined to 2.0 A resolution

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MAX IV BEAMLINE BioMAX
Synchrotron site	MAX IV
Beamline	BioMAX
Temperature [K]	100
Detector technology	PIXEL
Collection date	2020-12-12
Detector	DECTRIS EIGER X 16M
Wavelength(s)	0.9763
Spacegroup name	P 1 21 1
Unit cell lengths	46.233, 53.947, 115.038
Unit cell angles	90.00, 99.77, 90.00

Refinement procedure

Resolution	39.990 - 2.000
R-factor	0.1827
Rwork	0.181
R-free	0.22000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	7pfl
Data reduction software	XDS (20200417)
Data scaling software	Aimless (0.7.4)
Phasing software	PHASER (2.8.3)
Refinement software	PHENIX (1.18.2)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	48.710	48.710	2.050
High resolution limit [Å]	2.000	8.940	2.000
Rmerge	0.095	0.046	1.693
Rmeas	0.104	0.050	1.860
Rpim	0.040	0.020	0.759
Total number of observations	247542	2781	16109
Number of reflections	38028	456	2783
<I/σ(I)>	9.7	26	1
Completeness [%]	99.9	99	100
Redundancy	6.5	6.1	5.8
CC(1/2)	0.998	0.998	0.394

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	20% w/v PEG 3350 200 mM Potassiumthiocyanate 100 mM Bis-Tris Propane pH 8.5