3OVL
Structure of an amyloid forming peptide VQIVYK from the TAU protein in complex with orange G
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 | 2008-11-17 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9792 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 55.056, 4.831, 22.127 |
| Unit cell angles | 90.00, 102.98, 90.00 |
Refinement procedure
| Resolution | 26.820 - 1.810 |
| R-factor | 0.2589 |
| Rwork | 0.259 |
| R-free | 0.25900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.220 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER (2.1.4) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 90.000 | 90.000 | 1.940 |
| High resolution limit [Å] | 1.800 | 3.080 | 1.800 |
| Rmerge | 0.179 | 0.163 | 0.433 |
| Number of reflections | 587 | ||
| <I/σ(I)> | 4.5 | ||
| Completeness [%] | 87.6 | 97.5 | 71 |
| Redundancy | 2.4 | 2.9 | 1.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 291 | reservoir contained 0.1M Zinc Acetate dihydrate, 18% PEG 3350, vapor diffusion, hanging drop, temperature 291K |
