2VVY

Structure of Vaccinia virus protein B14

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM14
Synchrotron site	ESRF
Beamline	BM14
Temperature [K]	100
Detector technology	CCD
Collection date	2005-07-08
Detector	MARRESEARCH
Spacegroup name	C 1 2 1
Unit cell lengths	168.673, 43.884, 99.878
Unit cell angles	90.00, 112.09, 90.00

Refinement procedure

Resolution	46.273 - 2.693
R-factor	0.2236
Rwork	0.223
R-free	0.24390
Structure solution method	MAD
Starting model (for MR)	NONE
RMSD bond length	0.005
RMSD bond angle	0.777
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	HKL2Map
Refinement software	PHENIX ((PHENIX.REFINE))

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.800
High resolution limit [Å]	2.700	2.700
Rmerge	0.120	0.840
Number of reflections	19127
<I/σ(I)>	10.4	1.8
Completeness [%]	99.8	98.6
Redundancy	3.7	3.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		294	SITTING DROPS CONTAINING 100 NL PROTEIN (3.2 MG/ML IN 50 MM TRIS PH 8.5, 150 MM NACL, 2 MM 2-MERCAPTOETHANOL) AND 100 NL RESERVOIR SOLUTION (0.2 M DIAMMONIUM TARTRATE, 20% (W/V) PEG 3350, 0.4 M NON-DETERGENT SULPHOBETANE 201 AND 2 MM 2-MERCAPTOETHANOL) WERE EQUILIBRATED AGAINST 95 UL RESERVOIRS AT 21 C. CRYSTALS WERE CRYOPROTECTED IN RESERVOIR SOLUTION SUPPLEMENTED WITH 20% (V/V) GLYCEROL.