4EIT

Crystal structure of an enoyl-(acyl carrier protein) reductase from Bartonella henselae

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-D
Synchrotron site	APS
Beamline	21-ID-D
Temperature [K]	100
Detector technology	CCD
Collection date	2012-03-28
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	1.07806
Spacegroup name	C 1 2 1
Unit cell lengths	122.360, 76.860, 171.950
Unit cell angles	90.00, 107.99, 90.00

Refinement procedure

Resolution	50.000 - 2.400
R-factor	0.1972
Rwork	0.196
R-free	0.22620
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3grk
RMSD bond length	0.012
RMSD bond angle	1.484
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER (2.3.0)
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000		2.460
High resolution limit [Å]	2.400	10.730	2.400
Rmerge	0.089	0.050	0.441
Number of reflections	59084	697	4292
<I/σ(I)>	10.42	20.88	3.14
Completeness [%]	99.1	96.1	98.6
Redundancy	3.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8	289	BaheA.00010.b.A1 PW26981 selenomethionine-labeled at 27.5 mg/mL against PACT screen condition B5, 0.1 M MIB pH 8.0, 25% PEG 1500 with 15% ethylene glycol as cryo-protectant, crystal tracking ID 232038b5, VAPOR DIFFUSION, SITTING DROP, temperature 289K