4IEL

Crystal structure of a glutathione s-transferase family protein from burkholderia ambifaria, target efi-507141, with bound glutathione

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	2012-07-09
Detector	RAYONIX MX225HE
Wavelength(s)	0.9793
Spacegroup name	C 2 2 21
Unit cell lengths	100.040, 170.730, 50.781
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	27.355 - 1.600
R-factor	0.188
Rwork	0.186
R-free	0.21620
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3m3m
RMSD bond length	0.007
RMSD bond angle	1.076
Data reduction software	MOSFLM
Data scaling software	SCALA (3.3.20)
Phasing software	BALBES
Refinement software	PHENIX (1.8.1_1168)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	86.314	27.355	1.690
High resolution limit [Å]	1.600	5.060	1.600
Rmerge		0.029	0.705
Total number of observations		12978	61742
Number of reflections	57737
<I/σ(I)>	11.5	19.8	1.1
Completeness [%]	99.9	96.7	100
Redundancy	7.4	6.8	7.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		298	Protein (10 mM Hepes pH 7.5, 150 mM NaCl, 5% glycerol). Reservoir (0.2 M MgFormate pH 5.9, 20% peg3350). Cryoprotection (Reservoir + 20% diethylene glycol), VAPOR DIFFUSION, SITTING DROP, temperature 298K