2VVW

Structure of Vaccinia virus protein A52

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-4
Synchrotron site	ESRF
Beamline	ID14-4
Temperature [K]	100
Detector technology	CCD
Collection date	2007-08-27
Detector	ADSC CCD
Spacegroup name	P 1 21 1
Unit cell lengths	46.208, 59.144, 75.719
Unit cell angles	90.00, 106.58, 90.00

Refinement procedure

Resolution	33.770 - 1.900
R-factor	0.179
Rwork	0.177
R-free	0.21500
Structure solution method	MAD
Starting model (for MR)	NONE
RMSD bond length	0.010
RMSD bond angle	1.107
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	autoSHARP
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.930
High resolution limit [Å]	1.900	1.900
Rmerge	0.080	0.710
Number of reflections	30971
<I/σ(I)>	12.1	1.9
Completeness [%]	99.9	99.7
Redundancy	4.1	4.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP		294	HANGING DROPS CONTAINING 1 UL PROTEIN (5.3 MG/ML IN 20 MM TRIS, 200 MM NACL, PH 7.5) AND 1 UL RESERVOIR SOLUTION (0.2 M TRISODIUM CITRATE, 18% (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.