3GQT

Crystal structure of glutaryl-CoA dehydrogenase from Burkholderia pseudomallei with fragment (1,4-dimethyl-1,2,3,4-tetrahydroquinoxalin-6-yl)methylamine

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.3
Synchrotron site	ALS
Beamline	5.0.3
Temperature [K]	100
Detector technology	CCD
Collection date	2009-03-02
Detector	ADSC QUANTUM 315
Wavelength(s)	0.97
Spacegroup name	P 21 21 21
Unit cell lengths	97.418, 106.374, 144.774
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 1.990
R-factor	0.202
Rwork	0.200
R-free	0.23800
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3d6b
RMSD bond length	0.015
RMSD bond angle	1.431
Data reduction software	HKL-2000
Data scaling software	HKL-2000
Phasing software	MOLREP
Refinement software	REFMAC (5.5.0088)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.060
High resolution limit [Å]	1.990	1.990
Rmerge	0.073	0.686
Number of reflections	103621
<I/σ(I)>	10.1
Completeness [%]	100.0	100
Redundancy	7.2	6.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	289	20% PEG 3000, 0.1M HEPES pH 7.5, 0.2M NaCl. Soaked overnight with 25 mM (1,4-dimethyl-1,2,3,4-tetrahydroquinoxalin-6-yl)methylamine, VAPOR DIFFUSION, SITTING DROP, temperature 289K