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

• Published in: Data in brief Vol. 8; pp. 108 - 113
• Main Authors: Selivanova, Olga M., Grigorashvili, Elizaveta I., Suvorina, Mariya Yu, Dzhus, Ulyana F., Nikulin, Alexey D., Marchenkov, Victor V., Surin, Alexey K., Galzitskaya, Oxana V.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier Inc 01.09.2016; Elsevier
• Subjects: Data
• ISSN: 2352-3409; 2352-3409
• DOI: 10.1016/j.dib.2016.05.020

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 Aβ40 and Aβ42” (Dovidchenko et al., 2016) [1]. Aβ peptide is one of the most intensively studied amyloidogenic peptides. Despite the huge number of articles devoted to studying different fragments of Aβ peptide there are only several papers with correct kinetics data, also there are a few papers with X-ray data, especially for Aβ42. Our data present X-ray diffraction patterns both for Aβ40 and Aβ42 as well for Tris–HCl and wax. Moreover, our data provide kinetics of amyloid formation by recombinant Аβ40 and synthetic Аβ42 peptides by using electron microscopy.