5TF4

Crystal structure of enoyl-(acyl carrier protein) reductase from Bartonella henselae in complext with NAD

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	2009-07-06
Detector	RAYONIX MX-300
Wavelength(s)	0.97856
Spacegroup name	C 1 2 1
Unit cell lengths	122.440, 76.860, 171.600
Unit cell angles	90.00, 107.73, 90.00

Refinement procedure

Resolution	40.863 - 1.950
R-factor	0.1516
Rwork	0.151
R-free	0.18690
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4eit
RMSD bond length	0.007
RMSD bond angle	0.835
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX (1.11rc1_2513)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	49.000	49.000	2.000
High resolution limit [Å]	1.950	8.720	1.950
Rmerge	0.060	0.020	0.567
Number of reflections	110388
<I/σ(I)>	16.46	49.87	2.87
Completeness [%]	99.7	94.9	99.6
Redundancy	3.81		3.82
CC(1/2)	0.999	0.999	0.854

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	290	RigakuReagents JCSG+ screen, B12: 20% PEG 3350, 200mM Potassium citrate tribasic; BaheA.00010.b.A1.PW25955 at 20.8mg/ml + 4mM NAD; cryo: 20% EG + 8mM NAD; tray 274390b12, puck yts5-10; GOL close to NAD tentatively modeled, purification buffer contains GOL