2F8A
Crystal structure of the selenocysteine to glycine mutant of human glutathione peroxidase 1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X10SA |
| Synchrotron site | SLS |
| Beamline | X10SA |
| Temperature [K] | 77 |
| Detector technology | CCD |
| Collection date | 2005-11-19 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.9791 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 127.592, 59.376, 81.132 |
| Unit cell angles | 90.00, 119.41, 90.00 |
Refinement procedure
| Resolution | 70.710 - 1.500 |
| R-factor | 0.13803 |
| Rwork | 0.138 |
| R-free | 0.15636 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1gp1 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.414 |
| 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] | 70.710 | 1.580 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.540 | 0.306 |
| Number of reflections | 80997 | |
| <I/σ(I)> | 15.4 | 2.9 |
| Completeness [%] | 95.7 | 75.2 |
| Redundancy | 3.5 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 293 | 35% TACSIMATE, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
