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) |