4HI7

Crystal structure of glutathione transferase homolog from drosophilia mojavensis, TARGET EFI-501819, 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	2012-08-13
Detector	RAYONIX MX225HE
Wavelength(s)	0.9793
Spacegroup name	P 31 2 1
Unit cell lengths	50.700, 50.700, 289.473
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	30.104 - 1.250
R-factor	0.2013
Rwork	0.200
R-free	0.22780
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2il3
RMSD bond length	0.011
RMSD bond angle	1.407
Data reduction software	MOSFLM
Data scaling software	SCALA (3.3.20)
Phasing software	PHENIX (1.8_1069)
Refinement software	PHENIX (1.8_1069)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	96.491	3.950	1.320
High resolution limit [Å]	1.250	2.800	1.250
Rmerge	0.073	0.053	0.457
Total number of observations		51136	55616
Number of reflections	116694
<I/σ(I)>	10.8	11.3	1.7
Completeness [%]	96.1	99.5	91.6
Redundancy	4.7	7.1	3.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	sitting drop vapor diffution	6.5	298	Protein (10 mM Hepes pH 7.5, 100 mM NaCl), Reservoir (0.2 M NaCl, 0.1 M Tris-CL pH 6.5, 30% PEG3000), Cryoprotection (reservoir + 20% ethylene glycol), sitting drop vapor diffution, temperature 298K