9F2H

Crystal structure of SARS-CoV-2 N-protein C-terminal domain in complex with riluzole

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID23-1
Synchrotron site	ESRF
Beamline	ID23-1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2021-07-10
Detector	DECTRIS EIGER2 X CdTe 16M
Wavelength(s)	0.774899
Spacegroup name	I 1 2 1
Unit cell lengths	93.056, 43.383, 109.326
Unit cell angles	90.00, 91.44, 90.00

Refinement procedure

Resolution	46.560 - 1.300
R-factor	0.16856
Rwork	0.168
R-free	0.18898
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.006
RMSD bond angle	1.360
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]	46.560	1.320
High resolution limit [Å]	1.300	1.300
Rpim	0.026	0.363
Number of reflections	103602	4726
<I/σ(I)>	12.3	1.9
Completeness [%]	97.0	89.9
Redundancy	5.5	4.7
CC(1/2)	0.999	0.685

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	291	PEG 3350 38%, 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. Soaking o/n with saturated concentration of riluzole in PEG 3350 40%, 0.1 M Tris pH 8.5, 50 mM ammonium sulfate, 1 mM InsP6 condition.