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 |