4XI8

Crystal Structure of the FIC domain of Bep5 protein (VirB-translocated Bartonella effector protein) from Bartonella clarridgeiae

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-G
Synchrotron site	APS
Beamline	21-ID-G
Temperature [K]	100
Detector technology	CCD
Collection date	2014-07-02
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97857
Spacegroup name	P 21 21 2
Unit cell lengths	99.270, 122.860, 143.710
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	46.021 - 2.950
R-factor	0.2373
Rwork	0.235
R-free	0.27890
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2vza
RMSD bond length	0.002
RMSD bond angle	0.539
Data scaling software	XSCALE
Phasing software	BALBES
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000		3.030
High resolution limit [Å]	2.950	13.190	2.950
Rmerge	0.075	0.029	0.516
Rmeas	0.082	0.033	0.562
Total number of observations	229118
Number of reflections	37608	436	2729
<I/σ(I)>	17.35	34.1	3.7
Completeness [%]	99.7	88.1	100
Redundancy	6.1		6.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	289	19.9 mg/mL protein, 1:1 with Wiz3/4(g5): 20% PEG3350, 0.1 M sodium citrate/citric acid, pH 4.0, 0.2 M sodium citrate tribasic