4YQU

Glutathione S-transferase Omega 1 bound to covalent inhibitor C1-31

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-G
Synchrotron site	APS
Beamline	21-ID-G
Temperature [K]	100
Detector technology	CCD
Collection date	2012-10-11
Detector	RAYONIX MX-300
Wavelength(s)	0.9786
Spacegroup name	P 1 21 1
Unit cell lengths	62.645, 72.588, 65.310
Unit cell angles	90.00, 112.69, 90.00

Refinement procedure

Resolution	45.220 - 1.940
R-factor	0.2049
Rwork	0.203
R-free	0.24030
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1eem
RMSD bond length	0.010
RMSD bond angle	0.940
Data scaling software	HKL-2000
Refinement software	BUSTER-TNT (BUSTER 2.11.2)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	50.000	50.000	1.970
High resolution limit [Å]	1.940	5.260	1.940
Rmerge	0.074	0.063	0.343
Total number of observations	114158
Number of reflections	36745
<I/σ(I)>	16
Completeness [%]	93.4	93.6	97.5
Redundancy	3.1	3.2	2.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	293	The GSTO1-C1-31 complex was concentrated to 23.9 mg/mL prior to crystallization. Crystals formed from drops containing equal volumes of complex and well solution (22.5% PEG 3350, 90 mM MES pH 6.5 and 4% tert-butanol).