1RPH
STRUCTURES OF RNASE A COMPLEXED WITH 3'-CMP AND D(CPA): ACTIVE SITE CONFORMATION AND CONSERVED WATER MOLECULES
Experimental procedure
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 64.750, 64.750, 65.210 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 10.000 - 2.200 |
| R-factor | 0.158 |
| RMSD bond length | 0.016 |
| RMSD bond angle | 0.027 |
| Refinement software | RESTRAIN |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 10.000 * |
| High resolution limit [Å] | 2.200 * |
| Rmerge | 0.034 * |
| Total number of observations | 16249 * |
| Number of reflections | 7698 * |
| Completeness [%] | 93.3 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 6 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 35 (mg/ml) | |
| 2 | 1 | drop | sodium phosphate | 20 (mM) | |
| 3 | 1 | drop | sodium acetate | 20 (mM) | |
| 4 | 1 | reservoir | ammonium sulfate | 35 (%) | |
| 5 | 1 | reservoir | sodium chlorine | 1.5 (M) |






