1GP1
THE REFINED STRUCTURE OF THE SELENOENZYME GLUTATHIONE PEROXIDASE AT 0.2-NM RESOLUTION
Experimental procedure
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 90.400, 109.500, 58.200 |
| Unit cell angles | 90.00, 99.00, 90.00 |
Refinement procedure
| Resolution | 6.000 - 2.000 |
| R-factor | 0.171 * |
| Rwork | 0.171 |
| RMSD bond length | 0.013 |
| RMSD bond angle | 2.100 |
| Refinement software | EREF |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 2.000 * |
| Rmerge | 0.101 * |
| Total number of observations | 93223 * |
| Number of reflections | 26564 * |
| Completeness [%] | 71.0 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Microdialysis * | 7.2 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | 2 (mM) | ||
| 2 | 1 | 1 | phosphate | 5 (mM) |






