6FSB

Influenza B/Memphis/13/03 endonuclease with I38T mutation

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	2017-10-04
Detector	DECTRIS PILATUS3 2M
Wavelength(s)	0.966
Spacegroup name	P 1 21 1
Unit cell lengths	37.980, 61.450, 92.630
Unit cell angles	90.00, 95.47, 90.00

Refinement procedure

Resolution	46.104 - 1.800
R-factor	0.1988
Rwork	0.197
R-free	0.23610
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5fml
RMSD bond length	0.011
RMSD bond angle	1.043
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX ((1.13_2998: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.850
High resolution limit [Å]	1.800	1.800
Number of reflections	39336	5269
<I/σ(I)>	7.55	1.17
Completeness [%]	91.3	92.4
Redundancy	1.7	1.7
CC(1/2)	0.996	0.596

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