2J9H

Crystal structure of human glutathione-S-transferase P1-1 cys-free mutant in complex with S-hexylglutathione at 2.4 A resolution

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	MAX II BEAMLINE I911-2
Synchrotron site	MAX II
Beamline	I911-2
Temperature [K]	100
Detector technology	CCD
Collection date	2006-04-07
Detector	MARRESEARCH
Spacegroup name	P 43 21 2
Unit cell lengths	59.566, 59.566, 238.350
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	20.000 - 2.400
R-factor	0.253
Rwork	0.250
R-free	0.31000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	9gss
RMSD bond length	0.012
RMSD bond angle	1.507
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	MOLREP
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.460
High resolution limit [Å]	2.400	2.400
Rmerge	0.090	0.270
Number of reflections	16119
<I/σ(I)>	5.8	2.4
Completeness [%]	90.0	99
Redundancy	6.5	6.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.4		SITTING DROP VAPOUR TECHNIQUE, 1 MICROLITRE OF PROTEIN AT 10 MG/ML IN 20 MM TRIS-HCL, PH 8.0 CONTAINING 5MM S-HEXYLGLUTATHIONE WAS MIXED WITH 1 MICROLITRE OF RESERVOIR SOLUTION, COMPOSED OF 1.5M AMMONIUM SULFATE AND 100MM SODIUM CITRATE