4RIK
Amyloid forming segment, AVVTGVTAV, from the NAC domain of Parkinson's disease protein alpha-synuclein, residues 69-77
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-E |
| Synchrotron site | APS |
| Beamline | 24-ID-E |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-08-23 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9791 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 61.864, 4.799, 17.263 |
| Unit cell angles | 90.00, 104.13, 90.00 |
Refinement procedure
| Resolution | 30.000 - 1.854 |
| R-factor | 0.1802 |
| Rwork | 0.176 |
| R-free | 0.22110 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | poly alanine |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.123 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER (2.5.6) |
| Refinement software | REFMAC (5.0) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 100.000 | 100.000 | 1.920 |
| High resolution limit [Å] | 1.850 | 3.990 | 1.850 |
| Rmerge | 0.117 | 0.075 | 0.248 |
| Number of reflections | 521 | ||
| <I/σ(I)> | 11.1 | ||
| Completeness [%] | 97.7 | 100 | 97.7 |
| Redundancy | 4.1 | 3.5 | 4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 273 | 0.9M Ammonium Phosphate, 0.1M Sodium Acetate, pH 4.6, vapor diffusion, hanging drop, temperature 273K |
