3DGS
Changing the determinants of protein stability from covalent to non-covalent interactions by in-vitro evolution: a structural and energetic analysis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | BRUKER AXS MICROSTAR |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2005-10-10 |
| Detector | MAR scanner 345 mm plate |
| Wavelength(s) | 1.54 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 48.860, 92.210, 94.350 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.900 |
| Rwork | 0.216 |
| R-free | 0.26300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2g3p |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.500 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | AMoRE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.000 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.095 | 0.441 |
| Number of reflections | 40287 | |
| <I/σ(I)> | 13.8 | 3.8 |
| Completeness [%] | 99.5 | 96.5 |
| Redundancy | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 288 | 25-30% PEG 3350, 0.005M CaCl2, 0.2M NH4Cl, 0.1 Tris, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 288K |
