2ONV
Crystal Structure of the amyloid-fibril forming peptide GGVVIA derived from the Alzheimer's amyloid Abeta (Abeta37-42).
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID13 |
| Synchrotron site | ESRF |
| Beamline | ID13 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-12-17 |
| Detector | MAR CCD 165 mm |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 16.760, 41.134, 4.789 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.570 - 1.610 |
| R-factor | 0.235 |
| Rwork | 0.228 |
| R-free | 0.29900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Extended beta strand GGVVIA |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.859 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 90.000 | 1.720 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.192 | 0.420 |
| Number of reflections | 532 | |
| <I/σ(I)> | 12.6 | |
| Completeness [%] | 96.7 | 96.7 |
| Redundancy | 4.5 | 4.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 291 | Peptide concentration: 15.0 mg/ml, Peptide:reservoir:additive ratio 5:4:1, Reservoir: 2.0M Ammonium sulfate, Additive: 3.0% 0.1M hexamine cobalt (III) chloride , VAPOR DIFFUSION, HANGING DROP, temperature 291K |
