6B9U

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

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	2017-03-22
Detector	RAYONIX MX-300
Wavelength(s)	0.97872
Spacegroup name	P 41 21 2
Unit cell lengths	88.130, 88.130, 111.950
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	41.643 - 1.800
R-factor	0.1616
Rwork	0.160
R-free	0.19950
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3n74
RMSD bond length	0.005
RMSD bond angle	0.838
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MoRDa
Refinement software	PHENIX (dev_2499)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	41.643	41.643	1.850
High resolution limit [Å]	1.800	8.050	1.800
Rmerge	0.045	0.023	0.510
Rmeas	0.048	0.025	0.547
Total number of observations	305083
Number of reflections	40952	535	2924
<I/σ(I)>	26.72	62.18	3.59
Completeness [%]	98.7	96.9	97.6
Redundancy	7.45	6.054	7.615
CC(1/2)	1.000	0.999	0.915

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	289	BrabA.00010.g.A1.PS00350 at 20.22 mg/mL with 4 mM NAD was mixed 1:1 with Morpheus (b8): 12.5% (w/v) PEG1000, 12.5% (w/v) PEG3350, 12.5% (v/v) MPD, 0.1 M MOPS/HEPES-Na pH 7.5, 0.03 M NaF, 0.03 M NaBr, 0.03 M NaI. Crystal was harvested direct from tray 271654b8 into puck mkn8-10.