4ONE

Crystal Structure of a 3-oxoacyl-[acyl-carrier protein] reductase from Brucella melitensis

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	2013-06-19
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	0.97857
Spacegroup name	P 1 21 1
Unit cell lengths	63.400, 125.520, 65.320
Unit cell angles	90.00, 104.69, 90.00

Refinement procedure

Resolution	63.180 - 1.650
R-factor	0.13335
Rwork	0.132
R-free	0.15495
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4da9
RMSD bond length	0.012
RMSD bond angle	1.484
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	REFMAC (5.8.0049)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	63.180		1.690
High resolution limit [Å]	1.650	7.380	1.650
Rmerge	0.045	0.027	0.253
Number of reflections	116611
<I/σ(I)>	18.33	40.56	3.93
Completeness [%]	98.5	96.9	87.4
Redundancy	3.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	289	JCSG+(d5): 70% MPD, 100mM HEPES free acid/ Sodium Hydroxide, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 289K