3BVG
Manipulating the coupled folding and binding process drives affinity maturation in a protein-protein complex
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2004-06-30 |
| Detector | RIGAKU RAXIS IV++ |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 42.700, 42.700, 287.142 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.000 |
| R-factor | 0.216 |
| Rwork | 0.213 |
| R-free | 0.27600 |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.755 |
| Data reduction software | CrystalClear |
| Data scaling software | CrystalClear |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 50.000 |
| High resolution limit [Å] | 2.000 |
| Rmerge | 0.063 |
| Number of reflections | 16498 |
| Completeness [%] | 86.0 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 298 | 0.1M Tris-Cl, pH 8.5, 2.4 M ammonium sulfate, 2.25% polyethylene glycol (PEG) 400 and 2.25% Tween 20, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
