9F2G

Crystal structure of SARS-CoV-2 N-protein C-terminal domain (apo form)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALBA BEAMLINE XALOC
Synchrotron site	ALBA
Beamline	XALOC
Temperature [K]	100
Detector technology	PIXEL
Collection date	2021-05-22
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.979260
Spacegroup name	P 1 21 1
Unit cell lengths	92.704, 45.140, 109.061
Unit cell angles	90.00, 93.96, 90.00

Refinement procedure

Resolution	48.420 - 1.570
R-factor	0.19093
Rwork	0.189
R-free	0.22854
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.007
RMSD bond angle	1.531
Data reduction software	XDS
Data scaling software	XDS
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0411)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	48.420	1.600
High resolution limit [Å]	1.570	1.570
Rpim	0.019	0.531
Number of reflections	123141	4598
<I/σ(I)>	21.2	1.2
Completeness [%]	97.4	74.1
Redundancy	6.4	4.7
CC(1/2)	0.999	0.647

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	291	PEG 3350 37%, 0.1 M Tris pH 8.5, 50 mM ammonium sulfate and 1 mM InsP6. Protein:precipitant ratio 1:1. Protein concentration: 16.5 mg/ml. Protein buffer: 20 mM Tris pH 8.0 and 150 mM NaCl.