5DAL

Crystal Structure of human Glutathione Transferase Pi complexed with a metalloid in the presence of Glutathione

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 14-BM-C
Synchrotron site	APS
Beamline	14-BM-C
Temperature [K]	100
Detector technology	CCD
Collection date	2005-11-17
Detector	ADSC QUANTUM 315
Wavelength(s)	0.9
Spacegroup name	C 1 2 1
Unit cell lengths	77.550, 90.220, 68.670
Unit cell angles	90.00, 98.01, 90.00

Refinement procedure

Resolution	34.000 - 1.500
R-factor	0.1813
Rwork	0.180
R-free	0.21250
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5gss
RMSD bond length	0.011
RMSD bond angle	1.396
Data scaling software	Aimless (0.5.8)
Phasing software	PHASER (2.5.3)
Refinement software	PHENIX ((phenix.refine: 1.8.2_1309))

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	35.630	35.630	1.530
High resolution limit [Å]	1.500	8.220	1.500
Rmerge	0.076	0.039	0.787
Rpim	0.032	0.021	0.317
Total number of observations	508961	1742	26101
Number of reflections	74367
<I/σ(I)>	15.2	56.7	2
Completeness [%]	99.5	73.6	99.4
Redundancy	6.8	4.9	7
CC(1/2)	0.995	0.973	0.638

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6	293	100MM MES, PH 6.0, 28% (W/V) PEG 8000, 20MM CACL2, 10MM DTT, 10MM GSH. Soaked in 2MM PAO dissolved in DMSO