5TS3

Crystal Structure of a 3-oxoacyl-[acyl-carrier protein] Reductase with bound NAD from Brucella melitensis

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	2016-04-20
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.97856
Spacegroup name	C 2 2 21
Unit cell lengths	83.070, 105.620, 126.040
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	34.680 - 1.550
R-factor	0.1466
Rwork	0.146
R-free	0.16950
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4nbr
RMSD bond length	0.006
RMSD bond angle	0.814
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	PHENIX

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	35.000	35.000	1.590
High resolution limit [Å]	1.550	6.930	1.550
Rmerge	0.073	0.037	0.524
Rmeas	0.081
Total number of observations	393292
Number of reflections	79835
<I/σ(I)>	14.53	34.58	2.93
Completeness [%]	99.3	95.1	98.1
Redundancy			4.5
CC(1/2)	0.998	0.998	0.829

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	290	BrmeB.00010.f.B1.PS01889 at 17.41 mg/ml, incubated with 4mM NAD, mixed 1:1 with an equal volume MCSG1(a1): 20% (w/v) PEG-8000, 0.1 M HEPES/NaOH, pH=7.5, cryoprotected with 20% ethylene glycol