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 |
