4KE3

Crystal structure of a glutathione transferase family member from Burkholderia graminis, target efi-507264, no gsh, disordered domains, space group P21, form(2)

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 MX-225
Wavelength(s)	0.9793
Spacegroup name	P 1 21 1
Unit cell lengths	78.211, 56.141, 98.299
Unit cell angles	90.00, 91.35, 90.00

Refinement procedure

Resolution	32.757 - 1.900
R-factor	0.155
Rwork	0.153
R-free	0.19880
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4kdx
RMSD bond length	0.012
RMSD bond angle	1.327
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	PHENIX (1.8.1_1168)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	100.000	100.000	1.930
High resolution limit [Å]	1.900	5.160	1.900
Rmerge	0.063	0.043	0.434
Number of reflections	68251
<I/σ(I)>	9.4
Completeness [%]	99.8	98.9	99.4
Redundancy	3.6	3.7	3.4

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 (0.15 M DL-Malic Acid, 20 %(w/v) PEG 3350); Cryoprotection (reservoir + 20% ethylene glycol), VAPOR DIFFUSION, SITTING DROP, temperature 298K