2P31
Crystal structure of human glutathione peroxidase 7
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 | 2007-03-03 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.95370 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 32.046, 56.224, 94.593 |
Unit cell angles | 90.00, 91.27, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.000 |
R-factor | 0.166 |
Rwork | 0.163 |
R-free | 0.21490 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2gs3 |
RMSD bond length | 0.015 |
RMSD bond angle | 1.432 |
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] | 32.040 | 2.110 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.144 | 0.575 |
Number of reflections | 22890 | |
<I/σ(I)> | 9 | 1.9 |
Completeness [%] | 100.0 | 100 |
Redundancy | 3.6 | 3.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 293 | 25% PEG 3350, 200 mM Ammoniun sulfate, 17% Glycerol, VAPOR DIFFUSION, SITTING DROP, temperature 293K |