1CQM
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 | 1999-05-06 |
| Detector | MARRESEARCH |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 51.081, 105.546, 80.838 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.650 |
| R-factor | 0.247 |
| Rwork | 0.247 |
| R-free | 0.25300 |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.300 |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.740 |
| High resolution limit [Å] | 1.650 | 1.650 |
| Rmerge | 0.056 | 0.243 |
| Number of reflections | 24926 | |
| <I/σ(I)> | 21.6 | |
| Completeness [%] | 94.6 | 94.6 |
| Redundancy | 3 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | unknown * | 8.5 | 293 | PEG 400, SODIUM CITRATE, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 20K |
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 | 30 (%) | |
| 4 | 1 | 1 | protein | 6-8 (mg/ml) |
