2PGT

CRYSTAL STRUCTURE OF HUMAN GLUTATHIONE S-TRANSFERASE P1-1[V104] COMPLEXED WITH (9R,10R)-9-(S-GLUTATHIONYL)-10-HYDROXY-9,10-DIHYDROPHENANTHRENE

Experimental procedure

Source type	ROTATING ANODE
Source details	RIGAKU RUH2R
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1996-04
Detector	RIGAKU RAXIS II
Spacegroup name	C 1 2 1
Unit cell lengths	80.180, 90.540, 69.370
Unit cell angles	90.00, 98.45, 90.00

Refinement procedure

Resolution	6.000 - 1.900
R-factor	0.183 *
Rwork	0.183
Structure solution method	DIFFERENCE FOURIER
Starting model (for MR)	1pgt
RMSD bond length	0.017
RMSD bond angle	0.034
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	GPRLSA

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.930
High resolution limit [Å]	1.900	1.900
Rmerge	0.059	0.287
Number of reflections	40456
<I/σ(I)>	12.31	1.77
Completeness [%]	95.5	77.3
Redundancy	3.9	1.45

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7		CRYSTALS WERE GROWN IN HANGING DROPS WHICH INITIALLY CONSISTED OF 5.9 MG/ML PROTEIN IN 0.1 M HEPES BUFFER (PH 7.0) CONTAINING 8.3 MM S-HEXYLGLUTATHIONE AND 1.0 M BUFFERED (PH 7.0) 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 7.0)., 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)