4KDU

Crystal structure of a glutathione transferase family member from Burkholderia graminis, target efi-507264, no gsh, ordered domains, space group P21, form(1)

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	2013-04-17
Detector	RAYONIX MX225HE
Wavelength(s)	0.9793
Spacegroup name	P 1 21 1
Unit cell lengths	65.603, 56.105, 67.216
Unit cell angles	90.00, 107.78, 90.00

Refinement procedure

Resolution	24.196 - 1.600
R-factor	0.1697
Rwork	0.168
R-free	0.20040
Structure solution method	FOURIER SYNTHESIS
RMSD bond length	0.011
RMSD bond angle	1.327
Data reduction software	MOSFLM
Data scaling software	SCALA (3.3.20)
Refinement software	PHENIX (1.8.1_1168)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	64.004	24.196	1.690
High resolution limit [Å]	1.600	5.060	1.600
Rmerge	0.083	0.044	0.261
Total number of observations		4829	22297
Number of reflections	57253
<I/σ(I)>	7.3	14	2.9
Completeness [%]	93.3	79.3	93.5
Redundancy	2.8	3	2.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4.5	298	Protein (10 mM Hepes pH 7.5, 150 mM NaCl, 5% glycerol, 5 mM GSH); Reservoir (1 M di-Ammonium Phosphate 0.1 M Sodium Acetate); Cryoprotection (reservoir + 20% glycerol), VAPOR DIFFUSION, SITTING DROP, temperature 298K