3BYY
Manipulating the coupled folding and binding process drives affinity maturation in a protein-protein complex
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X12B |
| Synchrotron site | NSLS |
| Beamline | X12B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-07-23 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.9902 |
| Spacegroup name | P 65 |
| Unit cell lengths | 96.690, 96.690, 91.840 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 50.000 - 2.200 |
| R-factor | 0.192 |
| Rwork | 0.190 |
| R-free | 0.23300 |
| RMSD bond length | 0.021 |
| RMSD bond angle | 1.739 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| 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 | 0.059 |
| Number of reflections | 27415 |
| Completeness [%] | 97.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 298 | 2.0 M ammonium sulfate, 0.1 M Tris-Cl pH 7.0, 0.3 % 1,6-diaminohexane, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
