4MF6

Crystal structure of glutathione transferase BgramDRAFT_1843 from Burkholderia graminis, Target EFI-507289, with two glutathione molecules bound per one protein subunit

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 31-ID
Synchrotron site	APS
Beamline	31-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2013-08-16
Detector	RAYONIX MX225HE
Spacegroup name	P 43 21 2
Unit cell lengths	84.175, 84.175, 78.597
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	50.000 - 1.200
R-factor	0.11273
Rwork	0.112
R-free	0.13111
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4ikh
RMSD bond length	0.010
RMSD bond angle	1.490
Data reduction software	HKL-3000
Data scaling software	HKL-3000
Phasing software	PHASER
Refinement software	REFMAC (5.8.0049)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	1.220
High resolution limit [Å]	1.200	1.200
Rmerge	0.096
Number of reflections	88463
<I/σ(I)>	6.3	2.3
Completeness [%]	100.0	100
Redundancy	13.6	10.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	8.5	298	protein in 10 mM HEPES, pH 7.5, 150 mM sodium chloride, 5% glycerol, reservoir: 0.1 M Tris-HCl, pH 8.5, 1.4 M ammonium tartrate dibasic, cryoprotectant: 20% ethylene glycol, VAPOR DIFFUSION, SITTING DROP, temperature 298K