5HFK

CRYSTAL STRUCTURE OF A GLUTATHIONE S-TRANSFERASE PROTEIN FROM ESCHERICHIA COLI OCh 157:H7 STR. SAKAI (ECs3186, TARGET EFI-507414) WITH BOUND GLUTATHIONE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 31-ID
Synchrotron site	APS
Beamline	31-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2014-06-13
Detector	RAYONIX MX225HE
Wavelength(s)	0.97931
Spacegroup name	P 41 21 2
Unit cell lengths	83.267, 83.267, 171.153
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	19.655 - 1.551
R-factor	0.1868
Rwork	0.185
R-free	0.21250
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3gx0
RMSD bond length	0.010
RMSD bond angle	1.188
Data reduction software	HKL-2000 (2.0.0)
Data scaling software	SCALEPACK (1.99.2)
Phasing software	PHASES (2.5.1)
Refinement software	PHENIX (1.9_1692)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	20.000	20.000	1.610
High resolution limit [Å]	1.550	3.330	1.550
Rmerge	0.093	0.066	0.421
Total number of observations	614788
Number of reflections	86041
<I/σ(I)>	11.6		2.653
Completeness [%]	98.2	99.6	92.5
Redundancy	7.1	11.9	3.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	298	Protein (18.49 mg/ml, 20 mM HEPES pH 7.5, 0.150 M Sodium Chloride, 5% v/v Glycerol, 4.5 mM DTT, 5 mM reduced Glutathione) were combined with an equal volume of Reservoir (100 mM Bis-tris pH 6.5, 100 mM Magnesium Chloride, 2.8 M Sodium Chloride); Cryoprotection (Equal volumes of Reservoir + 50% v/v Glycerol)