2Y29
Structure of segment KLVFFA from the amyloid-beta peptide (Ab, residues 16-21), alternate polymorph III
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-2 |
| Synchrotron site | ESRF |
| Beamline | ID23-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | MARMOSAIC 225 mm CCD |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 9.590, 12.070, 42.210 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.300 |
| R-factor | 0.22609 |
| Rwork | 0.224 |
| R-free | 0.26003 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.023 |
| RMSD bond angle | 1.519 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.6.0081) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.400 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.190 | 0.520 |
| Number of reflections | 266 | |
| <I/σ(I)> | 5.9 | 3.19 |
| Completeness [%] | 94.3 | 89.5 |
| Redundancy | 3.9 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8.5 | AB16-21 FORM III CRYSTALS WERE OBTAINED AFTER THE SEGMENT WAS DISSOLVED IN WATER AT 5 MG/ML AND MIXED WITH 0.2M AMMONIUM ACETATE, 0.1 M TRIS BUFFER PH 8.5 AND 30% ISOPROPANOL. |
