6WJI

2.05 Angstrom Resolution Crystal Structure of C-terminal Dimerization Domain of Nucleocapsid Phosphoprotein from SARS-CoV-2

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	100
Detector technology	CCD
Collection date	2020-04-09
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97872
Spacegroup name	P 21 21 21
Unit cell lengths	43.612, 122.317, 130.633
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.881 - 2.052
Rwork	0.187
R-free	0.22750
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2cjr
RMSD bond length	0.004
RMSD bond angle	1.493
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	PHASER
Refinement software	REFMAC (5.8.0258)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.090
High resolution limit [Å]	2.050	2.050
Rmerge	0.171	0.630
Rmeas	0.187	0.697
Rpim	0.073	0.288
Number of reflections	43336	1770
<I/σ(I)>	9.7	2.6
Completeness [%]	97.0	80.6
Redundancy	6.2	5.5
CC(1/2)	0.976	0.698

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	292	20.0 mg/mL protein in 0.1 M sodium chloride, 0.01 M Tris, pH 8.3 against Classics II screen D8 (0.1 M HEPES, pH 7.5, 25% w/v PEG3350)