3K74
Disruption of protein dynamics by an allosteric effector antibody
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SOLEIL BEAMLINE PROXIMA 1 |
| Synchrotron site | SOLEIL |
| Beamline | PROXIMA 1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-02-19 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 0.98 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 55.300, 62.322, 102.848 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 7.990 - 1.950 |
| R-factor | 0.198 |
| Rwork | 0.196 |
| R-free | 0.24000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDB entries 1HCV 5dfr |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.746 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.930 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.102 | 0.388 |
| Number of reflections | 28725 | |
| <I/σ(I)> | 12.5 | |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 7.1 | 7.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 8.5 | 298 | 40% v/v PEG300, 5% w/v PEG1000, 100 mM Tris-HCl, pH 8.5, VAPOR DIFFUSION, temperature 298K |
