2RSP
STRUCTURE OF THE ASPARTIC PROTEASE FROM ROUS SARCOMA RETROVIRUS REFINED AT 2 ANGSTROMS RESOLUTION
Experimental procedure
Spacegroup name | P 31 2 1 |
Unit cell lengths | 88.950, 88.950, 78.900 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 10.000 - 2.000 |
R-factor | 0.144 |
RMSD bond length | 0.022 |
RMSD bond angle | 0.062 |
Refinement software | PROFFT |
Data quality characteristics
Overall | |
High resolution limit [Å] | 2.000 * |
Rmerge | 0.069 * |
Total number of observations | 95106 * |
Number of reflections | 20613 * |
Completeness [%] | 86.0 * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | ammonium sulfate |