5JSC

Crystal structure of a Putative acyl-CoA dehydrogenase from Burkholderia xenovorans

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	2016-03-25
Detector	RAYONIX MX-225
Wavelength(s)	0.97872
Spacegroup name	P 1 21 1
Unit cell lengths	78.300, 73.750, 149.490
Unit cell angles	90.00, 99.66, 90.00

Refinement procedure

Resolution	45.004 - 1.500
R-factor	0.13
Rwork	0.130
R-free	0.16010
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5idu
RMSD bond length	0.005
RMSD bond angle	0.798
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	PHENIX (dev_2386)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000		1.540
High resolution limit [Å]	1.500	6.710	1.500
Rmerge	0.060	0.029	0.528
Number of reflections	266729
<I/σ(I)>	14.98	38.66	2.19
Completeness [%]	99.5	97.9	94.5
Redundancy	4.5
CC(1/2)	0.998

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4.2	290	RigakuReagents JCSG+ screen A6: 20% PEG 1000, 200mM Li2SO4, 50mM Na2HPO4/Citric acid pH4.2; BuxeA.00027.j.B1.PS37826 at 15mg/ml + 2.5mM CoA; cryo: 15% EG + 1mM CoA in 2 steps; tray 270711a6; puck vod9-4