1LBK

Crystal structure of a recombinant glutathione transferase, created by replacing the last seven residues of each subunit of the human class pi isoenzyme with the additional C-terminal helix of human class alpha isoenzyme

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2001-03-15
Detector	MARRESEARCH
Wavelength(s)	1.5418
Spacegroup name	P 21 21 21
Unit cell lengths	68.300, 79.300, 89.900
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	14.960 - 1.860
R-factor	0.198
Rwork	0.198
R-free	0.22400
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	7gss
RMSD bond length	0.005
RMSD bond angle	1.150 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	CNS (1.1)
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	15.000	1.930
High resolution limit [Å]	1.860	1.860
Rmerge	0.036	0.211
Total number of observations	158396 *
Number of reflections	41262
<I/σ(I)>	37.3	6.7
Completeness [%]	99.0	96.4
Redundancy	3.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6	22 *	PEG 8000, calcium chloride, glutathione, (R,R)-1,4-dithiothreitol, 2-[N-morpholino]ethanesulphonic acid, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	8.5 (mg/ml)
2	1	drop	phosphate	10 (mM)	pH7.0
3	1	drop	EDTA	0.1 (mM)
4	1	reservoir	PEG8000	20-25 (%(w/v))
5	1	reservoir	dithiothreitol	10 (mM)
6	1	reservoir	MES	100 (mM)	pH5.5-6.5
7	1	reservoir	GSH	1 (mM)