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 |