1BAO
THE CONTRIBUTION OF BURIED HYDROGEN BONDS TO PROTEIN STABILITY: THE CRYSTAL STRUCTURES OF TWO BARNASE MUTANTS
Experimental procedure
| Spacegroup name | P 32 |
| Unit cell lengths | 58.809, 58.809, 81.902 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 6.000 - 2.200 |
| R-factor | 0.152 |
| RMSD bond length | 0.018 |
| RMSD bond angle | 0.053 |
| Phasing software | X-PLOR |
| Refinement software | PROLSQ |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 6.000 * |
| High resolution limit [Å] | 2.200 * |
| Rmerge | 0.172 * |
| Total number of observations | 30016 * |
| Number of reflections | 14908 * |
| Completeness [%] | 92.3 * |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 15 (mg/ml) | |
| 2 | 1 | reservoir | phosphate | 2.8 (M) | |
| 3 | 1 | reservoir | 2 (mM) |






