2X6M
Structure of a single domain camelid antibody fragment in complex with a C-terminal peptide of alpha-synuclein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X11 |
| Temperature [K] | 173 |
| Detector technology | IMAGE PLATE |
| Detector | MAR555 FLAT PANEL |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 60.170, 63.120, 62.870 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 43.560 - 1.620 |
| R-factor | 0.1596 |
| Rwork | 0.156 |
| R-free | 0.20258 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1hcv |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.693 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.710 |
| High resolution limit [Å] | 1.620 | 1.620 |
| Rmerge | 0.120 | 0.540 |
| Number of reflections | 15482 | |
| <I/σ(I)> | 23.3 | 4.3 |
| Completeness [%] | 99.9 | 99.9 |
| Redundancy | 14.3 | 14.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | 25% PEG6000, 100 MM HEPES PH 7.5, 100 MM LICL |
