1N2A

Crystal Structure of a Bacterial Glutathione Transferase from Escherichia coli with Glutathione Sulfonate in the Active Site

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	113
Detector technology	IMAGE PLATE
Collection date	1997-09-10
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.54
Spacegroup name	P 21 21 21
Unit cell lengths	47.616, 57.166, 134.927
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.700 * - 1.900
R-factor	0.20089
Rwork	0.195
R-free	0.26000 *
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1aof
RMSD bond length	0.020
RMSD bond angle	1.860 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC (5.1.24)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	19.700
High resolution limit [Å]	1.900	1.900 *
Rmerge	0.041 *	0.220 *
Number of reflections	23318
Completeness [%]	86.8 *	41.6 *
Redundancy	11 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	4.7	20 *	PEG 3000, B-n-octyl-glucopyranoside, glutathione sulfonate, sodium acetate, pH 4.7, VAPOR DIFFUSION, SITTING DROP, temperature 298K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10-20 (mg/ml)
2	1	drop	glutathione sulfonate	3-5 (mM)
3	1	drop	beta-n-octylglucopyranoside	0.3 (%)
4	1	drop	PEG3000	7 (%)
5	1	reservoir	sodium acetate	0.1 (M)
6	1	reservoir	PEG3000	14-18 (%)	pH4.7