X-ray diffraction and electron microscopy data for amyloid formation of Aβ40 and Aβ42

• DOI: 10.1016/j.dib.2016.05.020
• Publication Date: 2016-05-21T23:00:54Z
• Authors: Olga M. Selivanova; Elizaveta I. Grig...; Mariya Yu. Suvorina; Ulyana F. Dzhus; Alexey D. Nikulin; Victor V. Marchenkov; Alexey K. Surin; Oxana V. Galzitskaya
• Keywords: Amyloid (mycology)

The data presented in this article are related to the research entitled "One of possible mechanisms amyloid fibrils formation based on sizes primary and secondary folding nuclei Aβ40 Aβ42" (Dovidchenko et al., 2016) [1]. Aβ peptide is one most intensively studied amyloidogenic peptides. Despite huge number articles devoted studying different fragments there only several papers with correct kinetics data, also a few X-ray especially for Aβ42. Our present diffraction patterns both Aβ42 as well Tris–HCl wax. Moreover, our provide by recombinant Аβ40 synthetic Аβ42 peptides using electron microscopy.