1BOX
N39S MUTANT OF RNASE SA FROM STREPTOMYCES AUREOFACIENS
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 293 |
| Detector technology | IMAGE PLATE |
| Collection date | 1997-07-15 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 41.490, 46.650, 51.650 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 14.900 - 1.600 |
| R-factor | 0.176 |
| Rwork | 0.181 |
| R-free | 0.21800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1rgg |
| RMSD bond length | 0.023 |
| RMSD bond angle | 0.040 |
| Data reduction software | DENZO |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 14.900 | 1.630 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.058 | 0.471 |
| Number of reflections | 12724 | |
| <I/σ(I)> | 30.1 | 1.9 |
| Completeness [%] | 92.1 | 57.1 |
| Redundancy | 4.8 | 2.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 8 | HANGING DROP VAPOUR EQUILIBRATION DROP: 10 MG/ML OF PROTEIN 0.1 M TRIS-HCL BUFFER AT PH 8.0 12,5 % PEG 6000 RESERVOIR: 25 % PEG 6000 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 0.1 (M) | |
| 3 | 1 | drop | PEG6000 | 12 (%) | |
| 4 | 1 | reservoir | PEG6000 | 25 (%) |
