1PA3

Crystal Structure of Glutathione-S-transferase from Plasmodium falciparum

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Detector technology	IMAGE PLATE
Collection date	2003-03-20
Detector	MARRESEARCH
Spacegroup name	P 21 21 2
Unit cell lengths	62.100, 88.200, 75.400
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	15.000 - 2.600 *
R-factor	0.23032
Rwork	0.228
R-free	0.25800 *
Structure solution method	MIR
RMSD bond length	0.008 *
RMSD bond angle	1.500 *
Refinement software	REFMAC (5.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000
High resolution limit [Å]	2.600	2.600
Rmerge	0.130 *	0.519 *
Number of reflections	13027 *
Completeness [%]	97.6 *	94.7 *
Redundancy	6.0 *	5.6 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6 *	298	Burmeister, C., (2003) Acta Cryst., D59, 1469. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	7 (mg/ml)
2	1	reservoir	ammonium sulfate	2.1 (M)
3	1	reservoir	sodium cacodylate	0.1 (M)	pH6.0
4	1	reservoir	glutathione	2 (mM)