3Q9N
In silico and in vitro co-evolution of a high affinity complementary protein-protein interface
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-05-11 |
| Detector | ADSC QUANTUM 210 |
| Spacegroup name | P 1 |
| Unit cell lengths | 53.122, 56.556, 56.977 |
| Unit cell angles | 89.78, 112.42, 90.03 |
Refinement procedure
| Resolution | 37.060 - 2.000 |
| R-factor | 0.192 |
| Rwork | 0.190 |
| R-free | 0.24000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDB ENTRIES 2D59 1mjo |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.119 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.5_2)) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 37.060 |
| High resolution limit [Å] | 2.000 |
| Number of reflections | 40222 |
| Completeness [%] | 98.0 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6 | 292 | 0.2 M LiCl 0.1 M MES, PEG 6000, VAPOR DIFFUSION, SITTING DROP, temperature 292K |
