4O49

Crystal structure of the vaccine antigen Transferrin Binding Protein B (TbpB) mutant Tyr-174-Ala from Actinobacillus pleuropneumoniae H87

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	CLSI BEAMLINE 08ID-1
Synchrotron site	CLSI
Beamline	08ID-1
Temperature [K]	100
Detector technology	CCD
Collection date	2009-12-17
Wavelength(s)	0.9795
Spacegroup name	C 2 2 21
Unit cell lengths	132.800, 150.400, 93.480
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	46.902 - 2.500
R-factor	0.1973
Rwork	0.197
R-free	0.20410
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.005
RMSD bond angle	0.822
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX (1.8.4_1496)

Data quality characteristics

	Overall
Low resolution limit [Å]	46.902
High resolution limit [Å]	2.500
Number of reflections	32675

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	293	0.16 M sodium acetate, 0.08 M calcium cacodylate, 23% PEG 3350, 15% glycerol, pH 6.5, vapor diffusion, hanging drop, temperature 293K