4IVF

Crystal structure of glutathione transferase homolog from Lodderomyces elongisporus, target EFI-501753, with two GSH per 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	2012-10-16
Detector	RAYONIX MX225HE
Wavelength(s)	0.9793
Spacegroup name	P 21 21 21
Unit cell lengths	90.598, 112.476, 194.384
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	37.126 - 2.200
R-factor	0.1592
Rwork	0.156
R-free	0.22340
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3gx0
RMSD bond length	0.007
RMSD bond angle	1.018
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]	194.384	40.022	2.320
High resolution limit [Å]	2.200	6.960	2.200
Rmerge		0.057	0.700
Total number of observations		22827	87431
Number of reflections	99618
<I/σ(I)>	7.1	10	1.1
Completeness [%]	98.5	98.6	97.9
Redundancy	6.1	6.7	6.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	5.6	298	Protein (10 mM Hepes pH 7.5, 100 mM NaCl); Reservoir (0.17M Amm Acetate, 0.085 M Sodium Citrate pH 5.6, 25.5% Peg4000, 15% (V/V) glycerol); Cryoprotection (Reservoir taken to 20% glycerol), vapor diffusion, sitting drop, temperature 298K