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 |