1RN1
THREE-DIMENSIONAL STRUCTURE OF GLN 25-RIBONUCLEASE T1 AT 1.84 ANGSTROMS RESOLUTION: STRUCTURAL VARIATIONS AT THE BASE RECOGNITION AND CATALYTIC SITES
Experimental procedure
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 91.710, 37.540, 77.670 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 6.000 - 1.840 |
| R-factor | 0.144 |
| Rwork | 0.144 |
| RMSD bond length | 0.018 |
| RMSD bond angle | 0.039 * |
| Phasing software | X-PLOR |
| Refinement software | PROLSQ |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 1.840 * |
| Rmerge | 0.046 * |
| Total number of observations | 53463 * |
| Number of reflections | 18062 * |
| Completeness [%] | 75.1 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 7 * | 20 * | micro seeding * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | 55 (%) | ||
| 2 | 1 | reservoir | potasssium phosphate | 0.1 (M) |






