8UA2

Crystal Structure of infected cell protein 0 (ICP0) from herpes simplex virus 1 (proteolyzed fragment)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 17-ID
Synchrotron site	APS
Beamline	17-ID
Temperature [K]	100
Detector technology	PIXEL
Collection date	2018-02-10
Detector	DECTRIS PILATUS 6M
Wavelength(s)	1.0000
Spacegroup name	P 41 21 2
Unit cell lengths	95.909, 95.909, 74.526
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	34.734 - 2.650
R-factor	0.2213
Rwork	0.218
R-free	0.28820
Structure solution method	SAD
RMSD bond length	0.009
RMSD bond angle	1.136
Data reduction software	XDS
Data scaling software	Aimless
Phasing software	CRANK2
Refinement software	PHENIX ((dev_3083: ???))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	47.950	2.780
High resolution limit [Å]	2.650	2.650
Rmerge	0.123	1.452
Rmeas	0.128	1.509
Rpim	0.036	0.410
Total number of observations	134156	18440
Number of reflections	10603	1373
<I/σ(I)>	14.6	1.9
Completeness [%]	100.0
Redundancy	12.7	13.4
CC(1/2)	0.999	0.862

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	291	PACT G3: 20% (w/v) PEG 3350, 100 mM Bis-Tris Propane pH 7.5, 200 mM NaI, 80% crystallization solution and 20% (v/v) PEG 200. The electron density was consistent with a protelyzed fragment spanning A636-Q776