4GCI

Crystal structure of glutahtione s-transferase homolog from yersinia pestis, target EFI-501894, with bound glutathione, monoclinic form

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	2012-07-20
Detector	RAYONIX MX-225
Wavelength(s)	0.9793
Spacegroup name	P 1 21 1
Unit cell lengths	48.741, 89.338, 57.546
Unit cell angles	90.00, 112.26, 90.00

Refinement procedure

Resolution	22.873 - 1.500
R-factor	0.1772
Rwork	0.176
R-free	0.20770
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	4g9h
RMSD bond length	0.005
RMSD bond angle	1.038
Data reduction software	MOSFLM
Data scaling software	SCALA (3.3.20)
Phasing software	PHENIX
Refinement software	PHENIX (1.8_1069)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	53.257	22.873	1.580
High resolution limit [Å]	1.500	4.740	1.500
Rmerge		0.041	0.577
Total number of observations		8458	39464
Number of reflections	72798
<I/σ(I)>	8.1	13	1.3
Completeness [%]	99.9	96.3	100
Redundancy	3.8	3.7	3.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	sitting drop vapor diffuction	5.5	298	Protein (10 mM Hepes pH 7.5, 100 mM NaCl); Reservoir (0.2 M Ammonium Acetate, 0.1 M Bis-Tris:HCl pH 5.5, 25% (w/v) PEG 3350); Cryoprotection (Reservoir, + 20% ethylene glycol), sitting drop vapor diffuction, temperature 298K