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Selivanova OM, Grigorashvili EI, Suvorina MY, et al. X-ray diffraction and electron microscopy data for amyloid formation of Aβ40 and Aβ42. Data Brief. 2016;8:108-13doi: 10.1016/j.dib.2016.05.020.
Selivanova, O. M., Grigorashvili, E. I., Suvorina, M. Y., Dzhus, U. F., Nikulin, A. D., Marchenkov, V. V., Surin, A. K., & Galzitskaya, O. V. (2016). X-ray diffraction and electron microscopy data for amyloid formation of Aβ40 and Aβ42. Data in brief, 8108-13. https://doi.org/10.1016/j.dib.2016.05.020
Selivanova, Olga M, et al. "X-ray diffraction and electron microscopy data for amyloid formation of Aβ40 and Aβ42." Data in brief vol. 8 (2016): 108-13. doi: https://doi.org/10.1016/j.dib.2016.05.020
Selivanova OM, Grigorashvili EI, Suvorina MY, Dzhus UF, Nikulin AD, Marchenkov VV, Surin AK, Galzitskaya OV. X-ray diffraction and electron microscopy data for amyloid formation of Aβ40 and Aβ42. Data Brief. 2016 May 20;8:108-13. doi: 10.1016/j.dib.2016.05.020. eCollection 2016 Sep. PMID: 27294177; PMCID: PMC4889875.
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Data Brief. 2016 May 20;8:108-13. doi: 10.1016/j.dib.2016.05.020. eCollection 2016 Sep.

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

Data in brief

Olga M Selivanova, Elizaveta I Grigorashvili, Mariya Yu Suvorina, Ulyana F Dzhus, Alexey D Nikulin, Victor V Marchenkov, Alexey K Surin, Oxana V Galzitskaya

Affiliations

  1. Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia.

PMID: 27294177 PMCID: PMC4889875 DOI: 10.1016/j.dib.2016.05.020

Abstract

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.

References

  1. J Struct Biol. 2016 Jun;194(3):404-14 - PubMed

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