1CQN
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 | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1999-02-27 |
Detector | MARRESEARCH |
Spacegroup name | P 64 2 2 |
Unit cell lengths | 82.821, 82.821, 141.583 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.000 - 2.100 |
R-factor | 0.218 |
Rwork | 0.218 |
R-free | 0.27600 |
RMSD bond length | 0.005 |
RMSD bond angle | 1.300 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.170 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.076 | 0.296 |
Number of reflections | 14676 | |
<I/σ(I)> | 11.1 | |
Completeness [%] | 84.0 | 83.2 |
Redundancy | 1.8 | 1.8 |
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) |