1UCL
Mutants of RNase Sa
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Temperature [K] | 120 |
| Detector technology | IMAGE PLATE |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 64.261, 77.658, 38.344 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 15.000 * - 1.820 |
| R-factor | 0.176 |
| Rwork | 0.176 |
| R-free | 0.21800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.004 |
| RMSD bond angle | 24.600 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | |
| High resolution limit [Å] | 1.820 |
| Rmerge | 0.062 * |
| Total number of observations | 98889 * |
| Number of reflections | 17544 * |
| Completeness [%] | 99.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.4 | 293 | 2.0M ammonium sulfate, 0.1M HEPES-Na pH 7.5, 2%(v/v) PEG400, pH 8.4, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | Tris | 0.1 (M) | pH8.4 |
| 2 | 1 | drop | protein | 10 (mg/ml) | |
| 3 | 1 | reservoir | ammonium sulfate | 2.0 (M) | |
| 4 | 1 | reservoir | sodium HEPES | 0.1 (M) | pH7.5 |
| 5 | 1 | reservoir | PEG400 | 2 (%(v/v)) |






