6T3Z

Crystal structure of the truncated EBV BFRF1-BFLF2 nuclear egress complex

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	BESSY BEAMLINE 14.2
Synchrotron site	BESSY
Beamline	14.2
Temperature [K]	100
Detector technology	PIXEL
Collection date	2017-05-12
Detector	DECTRIS PILATUS3 2M
Wavelength(s)	0.9184
Spacegroup name	P 61 2 2
Unit cell lengths	59.313, 59.313, 265.370
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	44.228 - 1.559
R-factor	0.214352796112
Rwork	0.212
R-free	0.24198
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5d5n
RMSD bond length	0.007
RMSD bond angle	0.788
Data reduction software	XDS
Data scaling software	XDS
Phasing software	PHASER
Refinement software	PHENIX (1.11.1_2575)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	47.900	1.617
High resolution limit [Å]	1.558	1.561
Rmeas	0.101	0.229
Number of reflections	40577	125
<I/σ(I)>	17.9
Completeness [%]	59.6	3.18
Redundancy	38
CC(1/2)	1.000	0.092

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		277.15	The protein was dissolved in a buffer consisting of 50 mM TrisHCl, 150 mM NaCl, pH 7.5 and concentrated to values between 10-15 mg/ml. Diffraction quality crystals of BFRF1::BFLF2 were obtained at 4 degree C with 0.2 M sodium malonate, pH 4.5, 20% PEG 3350 as a reservoir solution.