6T3X

Crystal structure of the truncated human cytomegalovirus pUL50-pUL53 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	2017-02-28
Detector	DECTRIS PILATUS3 2M
Wavelength(s)	0.918400
Spacegroup name	P 1 21 1
Unit cell lengths	37.270, 82.570, 63.660
Unit cell angles	90.00, 95.10, 90.00

Refinement procedure

Resolution	41.280 - 1.480
R-factor	0.1944
Rwork	0.192
R-free	0.22490
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5d5n
RMSD bond length	0.005
RMSD bond angle	0.784
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MLPHARE
Refinement software	PHENIX (1.13_2998)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	41.290	1.520
High resolution limit [Å]	1.480	1.480
Rmeas	0.090	0.929
Number of reflections	63159	4515
<I/σ(I)>	8.9	1.59
Completeness [%]	98.7	96.3
Redundancy	4	3.9
CC(1/2)	0.993	0.592

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		277	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 pUL50::pUL53 were obtained at 4 degree C with 20% PEG 4000, 10% propanol, 100 mM HEPES, pH 7.5 as a reservoir solution.