1E6B

Crystal structure of a Zeta class glutathione S-transferase from Arabidopsis thaliana

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX7.2
Synchrotron site	SRS
Beamline	PX7.2
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1999-10-17
Detector	MAR scanner 345 mm plate
Spacegroup name	P 65 2 2
Unit cell lengths	75.164, 75.164, 140.520
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	25.000 - 1.650
R-factor	0.196 *
Rwork	0.196
R-free	0.23400
Structure solution method	SIRAS
RMSD bond length	0.011
RMSD bond angle	1.600 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CCP4
Refinement software	REFMAC

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000	1.690
High resolution limit [Å]	1.650	1.650
Rmerge	0.040
Number of reflections	150341
Completeness [%]	94.7	95.9
Redundancy	5-6 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	7.5	15 *	11% PEG 8000, 0.2M MAGNESIUM ACETATE, 0.1 M SODIUM CACODYLA, pH 7.50

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	20 (mg/ml)
2	1	drop	Tris-HCl	20 (mM)
3	1	reservoir	PEG8000	11 (%(w/v))
4	1	reservoir	magnesium acetate	0.2 (M)
5	1	reservoir	sodium cacodylate	0.1 (M)