4U6H

Vaccinia L1/M12B9-Fab complex

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL11-1
Synchrotron site	SSRL
Beamline	BL11-1
Temperature [K]	100
Detector technology	PIXEL
Collection date	2013-05-29
Detector	DECTRIS PILATUS 6M
Wavelength(s)	0.97945
Spacegroup name	P 32 2 1
Unit cell lengths	102.829, 102.829, 238.355
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	47.210 - 3.100
R-factor	0.21221
Rwork	0.209
R-free	0.26491
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ypy 1sy6
RMSD bond length	0.004
RMSD bond angle	0.865
Refinement software	REFMAC (5.7.0029)

Data quality characteristics

	Overall
Low resolution limit [Å]	47.670
High resolution limit [Å]	3.100
Rmerge	0.200
Number of reflections	27308
<I/σ(I)>	9.7
Completeness [%]	99.9
Redundancy	9.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7	293	Initial crystallization experiments were carried out by sitting-drop vapor diffusion in a 96-well format, using a Phoenix liquid-handling robot with a panel of commercial sparse-matrix screens (PEG/Ion 1 and 2 from Hampton Research, Wizard 2 from Emerald Biosciences, JCSG Plus Suite from Qiagen, and JBScreen 6 from Jena BioScience). Quality diffracting crystals of L1/M12B9-Fab complex were obtained at RT by mixing 0.5ul of protein solution at 9.5 mg/ml with 0.5ul of precipitant [100 mM Tris, pH 7.0, 20% (w/v) polyethylene glycol (PEG) 3000, and 200 mM Ca(OAc)] and seeding with initial crystals obtained at 6.5 mg/ml. Crystal were flash-frozen at 100K in mother liquor containing 20 % glycerol.