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 |






