1RPF
THE STRUCTURES OF RNASE 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 | 65.250, 65.250, 65.520 | 
| Unit cell angles | 90.00, 90.00, 120.00 | 
Refinement procedure
| Resolution | 10.000 - 2.200 | 
| R-factor | 0.155 | 
| RMSD bond length | 0.018 | 
| RMSD bond angle | 0.033 | 
| Refinement software | RESTRAIN | 
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 10.000 *  | 
| High resolution limit [Å] | 2.200 *  | 
| Rmerge | 0.103 *  | 
| Total number of observations | 43289 *  | 
| Number of reflections | 8395 *  | 
| Completeness [%] | 99.7 *  | 
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) | 






