1QJH
Protein Aggregation and Alzheimer's Disease: Crystallographic Analysis of the Phenomenon. Engineered version of the ribosomal protein S6 used as a stable scaffold to study oligomerization.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I711 |
| Synchrotron site | MAX II |
| Beamline | I711 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 1999-02-15 |
| Detector | MARRESEARCH |
| Spacegroup name | P 42 21 2 |
| Unit cell lengths | 49.701, 49.701, 73.255 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 35.000 - 2.200 |
| R-factor | 0.205 |
| Rwork | 0.205 |
| R-free | 0.27500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ris |
| RMSD bond length | 0.008 |
| RMSD bond angle | 23.000 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (0.5) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.280 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.047 | 0.226 |
| Number of reflections | 5041 | |
| <I/σ(I)> | 35 | 11 |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 11.6 | 11.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | unknown * | 8.5 * | pH 7.00 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | 1 | sodium citrate | 0.2 (M) | |
| 2 | 1 | 1 | Tris | 0.1 (M) | pH8.5 |
| 3 | 1 | 1 | PEG400 | 20 (%) | |
| 4 | 1 | 1 | protein | 6-8 (mg/ml) |
