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. |