2C3Q

Human glutathione-S-transferase T1-1 W234R mutant, complex with S- hexylglutathione

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-1
Synchrotron site	ESRF
Beamline	ID14-1
Temperature [K]	100
Detector technology	CCD
Collection date	2004-09-03
Detector	ADSC CCD
Spacegroup name	P 21 21 21
Unit cell lengths	54.499, 109.683, 171.048
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	28.980 - 1.850
R-factor	0.224
Rwork	0.223
R-free	0.25200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2c3n
RMSD bond length	0.016
RMSD bond angle	1.779
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC (5.2.0005)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	1.900
High resolution limit [Å]	1.850	1.850
Rmerge	0.070	0.570
Number of reflections	82135
<I/σ(I)>	15	2.3
Completeness [%]	90.5	82.5
Redundancy	1.8	1.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	8		HANGING-DROP VAPOR-DIFFUSION TECHNIQUE, 5 MICROLITRES OF RESERVOIR SOLUTION [35% (V/V) PEG 3350, 200 MM MG(NO3)2, 200 MM NAI AND 2 MM DITHIOTHREITOL] WERE MIXED WITH 5 MICROLITRES OF PROTEIN SOLUTION (10 MG/ML IN 10 MM TRIS-HCL PH 7.8, 15 % GLYCEROL), 1 MICROLITRE 100 MM CACL2 AND 1 MICROLITRE 20 MM S-HEXYLGLUTATHIONE