5KEJ

Crystallographic structure of the Tau class glutathione S-transferase MiGSTU in complex with S-hexyl-glutathione

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL14-1
Synchrotron site	SSRL
Beamline	BL14-1
Temperature [K]	100
Detector technology	CCD
Collection date	2016-05-21
Detector	MARMOSAIC 325 mm CCD
Wavelength(s)	1.181
Spacegroup name	P 21 21 21
Unit cell lengths	64.319, 88.805, 96.583
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	40.343 - 2.350
R-factor	0.1895
Rwork	0.188
R-free	0.22610
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	Homology model based on the structure of wheat Tau class glutathione S-transferase (PDB entry 1GWC).
RMSD bond length	0.010
RMSD bond angle	1.219
Data reduction software	XDS
Data scaling software	SCALA
Phasing software	PHASER
Refinement software	PHENIX (1.9_1692)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	40.343	2.480
High resolution limit [Å]	2.350	2.350
Rmerge	0.170
Number of reflections	23652
<I/σ(I)>	11.8	3.3
Completeness [%]	100.0	100
Redundancy	14.6	14.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	BATCH MODE	6	289	0.2 M ammonium acetate, 0.1 M Bis-Tris pH 6.0, 25%(w/v) polyethylene glycol 3350, 5 mM S-hexyl-glutathione