3OW9
Structure of an amyloid forming peptide KLVFFA from amyloid beta, alternate polymorph II
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 | 2009-06-09 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9792 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 46.053, 9.561, 20.871 |
| Unit cell angles | 90.00, 97.43, 90.00 |
Refinement procedure
| Resolution | 22.830 - 1.800 |
| R-factor | 0.2127 |
| Rwork | 0.207 |
| R-free | 0.25750 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.180 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER (2.1.4) |
| Refinement software | BUSTER-TNT |
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 | 0.161 | 0.122 | 0.480 |
| Number of reflections | 849 | ||
| <I/σ(I)> | 4.5 | ||
| Completeness [%] | 90.9 | 88.2 | 81.2 |
| Redundancy | 3.2 | 3.4 | 2.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 291 | reservoir contained 30% (v/v) Jeffamine M-600, 0.1M Mes pH 6.5 ; 0.05M CsCl, 1mM FDDNP, vapor diffusion, hanging drop, temperature 291K |
