8KH2
Crystal structure of horse-spleen L-ferritin fused with amyloid beta peptide (1-42).
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU FR-E DW |
Temperature [K] | 93.1 |
Detector technology | PIXEL |
Collection date | 2023-08-09 |
Detector | RIGAKU HyPix-6000HE |
Wavelength(s) | 1.542 |
Spacegroup name | F 4 3 2 |
Unit cell lengths | 181.935, 181.935, 181.935 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 21.691 - 2.000 |
Rwork | 0.215 |
R-free | 0.25810 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.013 |
RMSD bond angle | 1.938 |
Data reduction software | CrysalisPro (v42) |
Data scaling software | Aimless (0.7.9) |
Phasing software | MOLREP (11.9.02) |
Refinement software | REFMAC (5.8.0415) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 21.691 | 2.050 |
High resolution limit [Å] | 2.000 | 2.000 |
Number of reflections | 17564 | 1264 |
<I/σ(I)> | 19.8 | |
Completeness [%] | 97.7 | |
Redundancy | 7.4 | |
CC(1/2) | 0.996 | 0.977 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293.15 | Ammonium sulfate (0.5-1.0M), Cadmium sulfate (12-20 mM) |