7K9P

Room temperature structure of NSP15 Endoribonuclease from SARS CoV-2 solved using SFX.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	FREE ELECTRON LASER
Source details	SLAC LCLS BEAMLINE MFX
Synchrotron site	SLAC LCLS
Beamline	MFX
Temperature [K]	295
Detector technology	PIXEL
Collection date	2020-09-02
Detector	SLAC ePix10k 2M
Wavelength(s)	1.277
Spacegroup name	P 63
Unit cell lengths	154.000, 154.000, 117.000
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	33.670 - 2.600
R-factor	0.19229
Rwork	0.191
R-free	0.20877
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	6xdh
RMSD bond length	0.006
RMSD bond angle	1.034
Data reduction software	CrystFEL (0.9.1)
Data scaling software	Aimless
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0258)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	33.670	2.690
High resolution limit [Å]	2.600	2.600
Number of reflections	48524	4435
<I/σ(I)>	3.1	0.2
Completeness [%]	100.0	100
Redundancy	101	70
CC(1/2)	0.940	0.030

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	BATCH MODE	5.5	295	NendoU protein 75 mg/ml (20 mM HEPES pH 7.5, 150mM NaCl, 1mM TCEP) is added to the precipitant solution (100mM Na Citrate pH 5.5, 20% PEG 1000, 20% 2-Methyl-2,4-pentanediol (MPD)) in a 1:7 protein:precipitant ratio with agitation at 295K overnight.