5VN6

Crystal structure of Taurine 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	2016-02-03
Detector	RAYONIX MX-300
Wavelength(s)	0.97872
Spacegroup name	C 1 2 1
Unit cell lengths	81.180, 84.890, 95.680
Unit cell angles	90.00, 110.53, 90.00

Refinement procedure

Resolution	40.465 - 2.100
R-factor	0.167
Rwork	0.165
R-free	0.20470
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3pvj
RMSD bond length	0.007
RMSD bond angle	0.888
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	MOLREP
Refinement software	PHENIX ((dev_2747))

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	40.465	40.465	2.150
High resolution limit [Å]	2.100	9.390	2.100
Rmerge	0.048	0.019	0.569
Rmeas	0.055	0.022	0.652
Number of reflections	35488	407	2598
<I/σ(I)>	19.4	52.51	2.82
Completeness [%]	99.7	95.1	99.9
Redundancy	4.21	3.6	4.252
CC(1/2)	0.999	0.999	0.836

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.65	290	RigakuReagents JCSG+ screen, D6: 18% PEG 8000, 100mM Tris base/HCl pH 7.65, 200mM MgCl2: BuamA.00024.a.B1.PS02503 at 20.9mg/ml : cryo: 20% EG: tray 267365D6, puck PRV7-6