4YQV

Glutathione S-transferase Omega 1 bound to covalent inhibitor C4-10

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 21-ID-D
Synchrotron site	APS
Beamline	21-ID-D
Temperature [K]	100
Detector technology	CCD
Collection date	2012-10-11
Detector	RAYONIX MX-300
Wavelength(s)	0.9786
Spacegroup name	C 1 2 1
Unit cell lengths	186.320, 71.373, 61.968
Unit cell angles	90.00, 105.16, 90.00

Refinement procedure

Resolution	44.960 - 2.060
R-factor	0.196
Rwork	0.195
R-free	0.22000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1eem
RMSD bond length	0.009
RMSD bond angle	0.920
Data scaling software	HKL-2000
Phasing software	MOLREP
Refinement software	BUSTER (2.10.2)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	50.000	2.140
High resolution limit [Å]	2.060	2.060
Rmerge	0.078	0.316
Number of reflections	46437
<I/σ(I)>	11.2
Completeness [%]	98.0	99.3
Redundancy	5	4.9

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	6.5	293	Complex was concentrated to 26.2 mg/mL. Crystals of the complex grew from sitting drops containing equal volumes of protein complex and well solution (22.5% PEG 3350, 90 mM MES pH 6.5 and 10 mM BaCl2).