5VXT

Crystal structure of catechol 1,2-dioxygenase from Burkholderia ambifaria

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	2016-08-03
Detector	RAYONIX MX-300
Wavelength(s)	0.97872
Spacegroup name	P 1 21 1
Unit cell lengths	66.080, 52.200, 105.190
Unit cell angles	90.00, 106.62, 90.00

Refinement procedure

Resolution	47.812 - 1.750
R-factor	0.1866
Rwork	0.186
R-free	0.22430
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1dmh
RMSD bond length	0.006
RMSD bond angle	0.778
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	PHENIX (dev_2744)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.800
High resolution limit [Å]	1.750	7.830	1.750
Rmerge	0.060	0.033	0.546
Rmeas	0.065	0.036	0.602
Number of reflections	69508	822	5101
<I/σ(I)>	18.24	42.63	2.73
Completeness [%]	99.8	97.2	99.4
Redundancy	6.216	5.647	5.602
CC(1/2)	0.999	0.999	0.914

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.6	290	MCSG1 C8 (274672c8): 200mM Ammonium sulfate, 100mM Sodium citrate: HCl, pH5.6, 25% (w/v) PEG4000, protein conc. 20.3mg/mL, cryo 20% ethylene glycol: ksj9-7