2R37
Crystal structure of human glutathione peroxidase 3 (selenocysteine to glycine mutant)
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 | 2007-07-15 |
Detector | MARRESEARCH |
Wavelength(s) | 1.00721 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 103.720, 61.308, 100.400 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 38.000 - 1.850 |
R-factor | 0.15269 |
Rwork | 0.151 |
R-free | 0.18263 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2i3y |
RMSD bond length | 0.014 |
RMSD bond angle | 1.414 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.3.0040) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 38.840 | 1.950 |
High resolution limit [Å] | 1.850 | 1.850 |
Rmerge | 0.086 | 0.664 |
Number of reflections | 226199 | |
<I/σ(I)> | 12.5 | 2.3 |
Completeness [%] | 99.9 | 100 |
Redundancy | 4.1 | 4.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8 | 277 | 0.1M PCB pH 8.0, 60% MPD, VAPOR DIFFUSION, SITTING DROP, temperature 277K |