4N5F

Crystal Structure of a Putative acyl-CoA dehydrogenase with bound FADH2 from Burkholderia cenocepacia J2315

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	2013-07-01
Detector	MARMOSAIC 300 mm CCD
Wavelength(s)	0.9786
Spacegroup name	P 43 21 2
Unit cell lengths	97.470, 97.470, 168.950
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.770 - 2.200
R-factor	0.183
Rwork	0.181
R-free	0.22370
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1jqi
RMSD bond length	0.012
RMSD bond angle	1.479
Data scaling software	XSCALE
Phasing software	PHASER (2.5.2)
Refinement software	REFMAC

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000		2.260
High resolution limit [Å]	2.200	9.840	2.200
Rmerge	0.063	0.028	0.562
Number of reflections	41958	513	3058
<I/σ(I)>	19.57	43.3	3.68
Completeness [%]	99.6	91.4	99.6
Redundancy	8.05

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	289	JCSG+(d10): 40% PEG-300, 100mM Sodium Cacodylate/HCl, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 289K