2GS3
Crystal structure of the selenocysteine to glycine mutant of human glutathione peroxidase 4(GPX4)
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 | 2006-03-24 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.95 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 62.945, 62.945, 195.984 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.900 |
| R-factor | 0.17251 |
| Rwork | 0.172 |
| R-free | 0.19080 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2f8a |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.361 |
| 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 | 2.000 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.096 | 0.415 |
| Number of reflections | 32109 | |
| <I/σ(I)> | 12.9 | 3.5 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 5.7 | 4.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.3 | 293 | 20% PEG 3350, 0.2 M ammonium chloride, pH 6.3, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
