4O3X

Crystal structure of the vaccine antigen Transferrin Binding Protein B (TbpB) mutant Phe-171-Ala from Actinobacillus pleuropneumoniae H49

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	P 61
Unit cell lengths	41.380, 41.380, 234.000
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	35.836 - 2.500
R-factor	0.1976
Rwork	0.195
R-free	0.24750
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.004
RMSD bond angle	0.787
Data reduction software	DENZO
Data scaling software	SCALEPACK
Refinement software	PHENIX (1.8.4_1496)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	2.610
High resolution limit [Å]	2.500	5.430	2.500
Rmerge	0.108	0.056	0.523
Number of reflections	7822
<I/σ(I)>	8.4
Completeness [%]	98.8	99.9	88.5
Redundancy	10.2	10.9	4.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8	293	0.1 M Tris, 0.2 M NaCl, 0.1 M KCl, 30% PEG MME 2000, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K