2OBI
Crystal structure of the Selenocysteine to Cysteine Mutant of human phospholipid hydroperoxide glutathione peroxidase (GPx4)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.1 |
| Synchrotron site | BESSY |
| Beamline | 14.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-08-29 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.9537 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 61.362, 61.362, 113.891 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 30.690 - 1.550 |
| R-factor | 0.1652 |
| Rwork | 0.164 |
| R-free | 0.18590 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1gp1 |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.276 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.1.19) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.610 |
| High resolution limit [Å] | 1.550 | 1.550 |
| Rmerge | 0.068 | 0.036 |
| Number of reflections | 35135 | |
| <I/σ(I)> | 32.07 | 2.48 |
| Completeness [%] | 95.6 | 66.6 |
| Redundancy | 9.4 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 295 | 15% PEG 8000, 0.1M MES buffer, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
