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) |