3Q2X
Structure of an amyloid forming peptide NKGAII (residues 27-32) from amyloid beta
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 | 2010-04-26 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 15.074, 4.838, 24.016 |
| Unit cell angles | 90.00, 95.56, 90.00 |
Refinement procedure
| Resolution | 23.903 - 1.451 |
| R-factor | 0.2095 |
| Rwork | 0.204 |
| R-free | 0.25890 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.869 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.6.1_357) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 100.000 | 100.000 | 1.500 |
| High resolution limit [Å] | 1.450 | 3.120 | 1.450 |
| Rmerge | 0.122 | 0.063 | 0.322 |
| Number of reflections | 671 | ||
| <I/σ(I)> | 11.3 | ||
| Completeness [%] | 90.9 | 86.5 | 94.6 |
| Redundancy | 3.1 | 2.9 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 291 | reservoir contained 2.4M Sodium Malonate, 15% v/v Glycerol, vapor diffusion, hanging drop, temperature 291K |
