4NPS

Crystal Structure of Bep1 protein (VirB-translocated Bartonella effector protein) from Bartonella clarridgeiae

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-F
Synchrotron site	APS
Beamline	21-ID-F
Temperature [K]	100
Detector technology	CCD
Collection date	2013-11-13
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.97857
Spacegroup name	P 21 21 2
Unit cell lengths	73.190, 97.850, 49.110
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	58.610 - 1.900
R-factor	0.1737
Rwork	0.172
R-free	0.21220
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2jk8
RMSD bond length	0.013
RMSD bond angle	1.502
Data scaling software	XSCALE
Phasing software	PHASER (2.5.5)
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	58.610		1.950
High resolution limit [Å]	1.900	8.500	1.900
Rmerge	0.036	0.016	0.522
Number of reflections	28414	341	2065
<I/σ(I)>	27.79	67.27	3.7
Completeness [%]	99.6	88.3	99.7
Redundancy	5.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	289	Morpheus(g5): 10% PEG-20,000, 20% PEG MME 550, 0.1M MOPS/HEPES-Na, pH=7.5, 0.02M each Sodium Formate, Ammonium Acetate, Trisodium Citrate, Sodium Potassium L-Tartrate, Sodium Oxamate, VAPOR DIFFUSION, SITTING DROP, temperature 289K