2I3Y
Crystal structure of human glutathione peroxidase 5
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 | 2006-06-19 |
Detector | MARRESEARCH |
Wavelength(s) | 0.8983 |
Spacegroup name | P 62 2 2 |
Unit cell lengths | 104.544, 104.544, 71.663 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 50.000 - 2.000 |
R-factor | 0.17718 |
Rwork | 0.175 |
R-free | 0.22835 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2f8a |
RMSD bond length | 0.015 |
RMSD bond angle | 1.458 |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((SCALA)) |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.110 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.064 | 0.417 |
Number of reflections | 16114 | |
<I/σ(I)> | 23 | 5.7 |
Completeness [%] | 99.9 | 100 |
Redundancy | 10.6 | 10.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8 | 293 | 20% PEG 3350, 0.2 M sodium formate, 5% ETHYLENE GLYCOL, pH 8, VAPOR DIFFUSION, SITTING DROP, temperature 293K |