4ISD

Crystal structure of GLUTATHIONE TRANSFERASE homolog from BURKHOLDERIA GL BGR1, TARGET EFI-501803, 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	2012-08-13
Detector	RAYONIX MX-225
Wavelength(s)	0.9793
Spacegroup name	C 2 2 21
Unit cell lengths	56.004, 196.343, 275.360
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	92.470 - 2.650
R-factor	0.201
Rwork	0.198
R-free	0.25430
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3bby
RMSD bond length	0.007
RMSD bond angle	1.074
Data reduction software	MOSFLM
Data scaling software	SCALA (3.3.20)
Phasing software	BALBES
Refinement software	PHENIX (1.8.1_1168)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	275.360	92.470	2.790
High resolution limit [Å]	2.650	8.380	2.650
Rmerge	0.095	0.035	0.869
Total number of observations		18847	96889
Number of reflections	43996
<I/σ(I)>	23.3	17.2	0.9
Completeness [%]	98.5	94.8	98.2
Redundancy	15	12.8	15.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	sitting drop vapor diffusion	7	298	Protein (10 mM Hepes pH 7.5, 25 mM NaCl, 5 mM Reduced glutathione), Reservoir (25% Sokalan CP7, 0.1 M KCl, 0.1 M HEPES pH 7), Cryoprotection (reservoir + 20% glycerol), sitting drop vapor diffusion, temperature 298K