4M16

Crystal Structure of the N-terminal Fic Domain of Bartonella effector protein (Bep); substrate of VirB T4SS (VirB-translocated Bep effector protein) from Bartonella sp. AR 15-3

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	2013-07-31
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.9786
Spacegroup name	P 1 21 1
Unit cell lengths	40.240, 47.480, 67.970
Unit cell angles	90.00, 105.64, 90.00

Refinement procedure

Resolution	38.780 - 1.850
R-factor	0.1665
Rwork	0.164
R-free	0.21090
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4lu4
RMSD bond length	0.014
RMSD bond angle	1.496
Data scaling software	XSCALE
Phasing software	PHASER (2.5.2)
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000		1.900
High resolution limit [Å]	1.850	8.270	1.850
Rmerge	0.059	0.015	0.552
Number of reflections	21213	251	1561
<I/σ(I)>	18.93	64.62	2.29
Completeness [%]	99.6	96.5	99.8
Redundancy	4.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	289	MCSG1(a1): 0.1 M HEPES/NaOH, pH 7.5, 20% PEG8000, VAPOR DIFFUSION, SITTING DROP, temperature 289K