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

The data presented in this article are related to the research article entitled One of the possible mechanisms of amyloid fibrils formation based on the sizes of primary and secondary folding nuclei of A beta 40 and A beta 42 (Dovidchenko et al., 2016) [1]. A beta peptide is one of the most intensively studied amyloidogenic peptides. Despite the huge number of articles devoted to studying different fragments of A beta peptide there are only several papers with correct kinetics data, also there are a few papers with X-ray data, especially for A beta 42. Our data present X-ray diffraction patterns both for A beta 40 and A beta 42 as well for Tris-HCl and wax. Moreover, our data provide kinetics of amyloid formation by recombinant A beta 40 and synthetic A beta 42 peptides by using electron microscopy. (C) 2016 The Authors. Published by Elsevier Inc. ocr