1PGT

CRYSTAL STRUCTURE OF HUMAN GLUTATHIONE S-TRANSFERASE P1-1[V104] COMPLEXED WITH S-HEXYLGLUTATHIONE

Experimental procedure

Source type	ROTATING ANODE
Source details	ENRAF-NONIUS FR571
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1996-03
Detector	MACSCIENCE
Spacegroup name	C 1 2 1
Unit cell lengths	79.390, 90.800, 69.150
Unit cell angles	90.00, 98.08, 90.00

Refinement procedure

Resolution	6.000 - 1.800
R-factor	0.182 *
Rwork	0.182
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1gss
RMSD bond length	0.015
RMSD bond angle	0.033
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	GPRLSA

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	1.830
High resolution limit [Å]	1.800	1.800
Rmerge	0.057	0.303
Number of reflections	43132
<I/σ(I)>	13.92	1.81
Completeness [%]	96.0	86.9
Redundancy	4.2	1.41

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5		CRYSTALS WERE GROWN IN HANGING DROPS WHICH INITIALLY CONSISTED OF 5.9 MG/ML PROTEIN IN 0.1 M HEPES BUFFER (PH 6.5) CONTAINING 8.3 MM S-HEXYLGLUTATHIONE AND 1.0 M BUFFERED (PH 6.5) AMMONIUM SULFATE. THE DROPS WERE EQUILIBRATED AT 293 K AGAINST WELL SOLUTION CONTAINING BETWEEN 1.9 - 2.0 M AMMONIUM SULFATE IN 0.1 M HEPES BUFFER (PH 6.5)., vapor diffusion - hanging drop

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	5.9 (mg/ml)
2	1	drop	HEPES	0.1 (M)
3	1	drop	GSHex	8.3 (mM)
4	1	drop	ammonium sulfate	1.0 (M)
5	1	reservoir	ammonium sulfate	1.9-2.0 (M)
6	1	reservoir	HEPES	0.1 (M)