6FS9

Influenza B/Memphis/13/03 endonuclease with I38T mutation with bound inhibitor, baloxavir acid (BXA)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE MASSIF-1
Synchrotron site	ESRF
Beamline	MASSIF-1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2017-10-18
Detector	DECTRIS PILATUS3 2M
Wavelength(s)	0.966
Spacegroup name	I 41
Unit cell lengths	63.710, 63.710, 125.410
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	56.800 - 2.280
R-factor	0.18177
Rwork	0.179
R-free	0.23541
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	PDB:5FML
RMSD bond length	0.016
RMSD bond angle	1.824
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	REFMAC (5.8.0189)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	56.800	2.340
High resolution limit [Å]	2.280	2.280
Number of reflections	10663
<I/σ(I)>	16.1	2.37
Completeness [%]	93.5
Redundancy	4.4
CC(1/2)	0.999	0.899

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		293	Protein, at 15-17 mg/ml, was incubated with 10-fold molar excess of BXA for 30 min at RT, mixtures were centrifuged at RT for 5 minutes at 12000 g, and soluble fraction was used for crystallization trials (final protein concentration 8-10 mg/ml). Mother liquor was 0.2 M CaCl2, 0.1 M MES pH 6.0, 20% (w/v) PEG6000