2HE3

Crystal structure of the selenocysteine to cysteine mutant of human glutathionine peroxidase 2 (GPX2)

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SLS BEAMLINE X10SA
Synchrotron site	SLS
Beamline	X10SA
Temperature [K]	100
Detector technology	CCD
Collection date	2006-05-18
Detector	MARRESEARCH
Wavelength(s)	0.9183
Spacegroup name	I 2 2 2
Unit cell lengths	41.308, 117.212, 120.157
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	42.000 - 2.100
R-factor	0.15833
Rwork	0.156
R-free	0.20481
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2f8a
RMSD bond length	0.016
RMSD bond angle	1.464
Phasing software	PHASER
Refinement software	REFMAC (5.2.0019)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	42.000	2.210
High resolution limit [Å]	2.100	2.100
Rmerge	0.137
Number of reflections	17619
<I/σ(I)>	14.9	3.2
Completeness [%]	99.8	98.7
Redundancy	9.1	6.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.5	293	20% PEG 3350, 200 mM sodium formate, 100 mM Bis-Tris propane, 10% ethylene glycol, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K