5KOI

Crystal Structure of a Possible Enoyl-(acyl-carrier-protein) Reductase from Brucella melitensis

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	CLSI BEAMLINE 08ID-1
Synchrotron site	CLSI
Beamline	08ID-1
Temperature [K]	100
Detector technology	CCD
Collection date	2016-05-27
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97949
Spacegroup name	P 1
Unit cell lengths	64.910, 83.830, 106.290
Unit cell angles	90.25, 100.08, 90.82

Refinement procedure

Resolution	48.675 - 1.700
R-factor	0.148
Rwork	0.146
R-free	0.17560
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3grk
RMSD bond length	0.006
RMSD bond angle	0.835
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000		1.740
High resolution limit [Å]	1.700	7.600	1.700
Rmerge	0.058	0.033	0.474
Number of reflections	236079
<I/σ(I)>	14.19	32.92	2.91
Completeness [%]	97.2	99.3	95.6
Redundancy	3.9		4
CC(1/2)	0.998	0.997	0.898

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		290	BrabA.00010.c.A1.PS000047 at 18.1 mg/ml, incubated with 4 mM NAD, protein mixed 1:1 and incubated with an equal volume PACT(a6): 25% (w/v) PEG-1500, 10 % (v/v) 10x SPG, pH=9, and cryoprotected with 20% ethylene glycol