2VVX

Structure of Vaccinia virus protein A52

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	DIAMOND BEAMLINE I03
Synchrotron site	Diamond
Beamline	I03
Temperature [K]	100
Detector technology	CCD
Collection date	2007-09-11
Detector	ADSC CCD
Spacegroup name	H 3
Unit cell lengths	126.075, 126.075, 124.058
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	40.981 - 2.746
R-factor	0.182
Rwork	0.181
R-free	0.19180
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2vvw CHAIN A
RMSD bond length	0.005
RMSD bond angle	0.816
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	PHASER
Refinement software	PHENIX ((PHENIX.REFINE))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.800
High resolution limit [Å]	2.750	2.750
Rmerge	0.090	0.820
Number of reflections	19184
<I/σ(I)>	13.8	2.1
Completeness [%]	100.0	100
Redundancy	5.7	4.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		294	HANGING DROPS CONTAINING 1 UL PROTEIN (5.4 MG/ML IN 20 MM TRIS, 200 MM NACL, PH 7.5) AND 1 UL RESERVOIR SOLUTION (0.2 M SODIUM PHOSPHATE, 22% (W/V) PEG 3350) WERE EQUILIBRATED AGAINST 500 UL RESERVOIRS AT 21 C. CRYSTALS WERE CRYOPROTECTED IN RESERVOIR SOLUTION SUPPLEMENTED WITH 20% (V/V) GLYCEROL.