1I4M
Crystal structure of the human prion protein reveals a mechanism for oligomerization
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1999-09-24 |
Detector | CUSTOM-MADE |
Wavelength(s) | 1.0688 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 85.441, 85.707, 40.501 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 * - 2.000 |
R-factor | 0.206 |
Rwork | 0.206 |
R-free | 0.25300 |
Structure solution method | MIR |
RMSD bond length | 0.008 * |
RMSD bond angle | 1.170 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MLPHARE |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.048 | 0.239 |
Number of reflections | 10069 | |
<I/σ(I)> | 36 | |
Completeness [%] | 96.7 | 84.8 |
Redundancy | 7.8 | 6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 8 | 20 * | SODIUM CHLORIDE, TRIS HYDROCHLORIDE, CADMIUM CHLORIDE, pH 8, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 5 (mg/ml) | |
2 | 1 | reservoir | Tris-HCl | 0.1 (M) | pH8. |
3 | 1 | reservoir | 3 (M) | ||
4 | 1 | reservoir | 5 (mM) |