3N74

Crystal structure of 3-ketoacyl-(acyl-carrier-protein) reductase from Brucella melitensis

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU FR-E+ SUPERBRIGHT
Temperature [K]	100
Detector technology	CCD
Collection date	2010-05-12
Detector	RIGAKU SATURN 944+
Wavelength(s)	1.5418
Spacegroup name	P 21 21 21
Unit cell lengths	70.520, 96.500, 130.340
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 2.200
R-factor	0.173
Rwork	0.170
R-free	0.23000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1cgo
RMSD bond length	0.014
RMSD bond angle	1.356
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER (2.1.4)
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.260
High resolution limit [Å]	2.200	2.200
Rmerge	0.147	0.508
Number of reflections	45847	3354
<I/σ(I)>	13.39	4.9
Completeness [%]	99.9	99.6
Redundancy	7.2	7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	9	289	40.4 mg/mL protein against PACT screen condition d6, 0.1 M MMT buffer pH 9, 25% PEG 1500, 25% ethylene glycol used as cryo-protectant, crystal tracking ID 205370d6, VAPOR DIFFUSION, SITTING DROP, temperature 289K