2Y2A
Structure of segment KLVFFA from the amyloid-beta peptide (Ab, residues 16-21), alternate polymorph I
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 | 9.580, 11.850, 42.470 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 11.410 - 1.910 |
| R-factor | 0.20837 |
| Rwork | 0.206 |
| R-free | 0.24787 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.703 |
| 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] | 21.200 | 2.200 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.150 | 0.360 |
| Number of reflections | 392 | |
| <I/σ(I)> | 7.4 | 3.85 |
| Completeness [%] | 85.0 | 75.7 |
| Redundancy | 3.5 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.5 | AB16-21 FORM I CRYSTALS WERE OBTAINED AFTER THE SEGMENT WAS DISSOLVED IN WATER AT 5 MG/ML AND MIXED WITH 0.2 M AMMONIUM ACETATE, 0.1 M BIS-TRIS PH 5.5, 45 % V/V MPD |
