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Ambiguities and completeness of SAS data analysis: investigations of apoferritin by SAXS/SANS EID and SEC-SAXS methods

Zabelskii, D. V. ; Vlasov, A. V. ; Ryzhykau, Yu L. ; Murugova, T. N. ; Brennich, M. ; Soloviov, D. V. ; Ivankov, O. I. ; Borshchevskiy, V. I. ; Mishin, A. V. ; Rogachev, A. V. ; Round, A. ; Dencher, N. A. ; Büldt, G. ; Gordeliy, V. I. ; Kuklin, A. I. (2018)
Ambiguities and completeness of SAS data analysis: investigations of apoferritin by SAXS/SANS EID and SEC-SAXS methods.
In: Journal of Physics: Conference Series, 994 (1)
doi: 10.1088/1742-6596/994/1/012017
Article, Bibliographie

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Abstract

The method of small angle scattering (SAS) is widely used in the field of biophysical research of proteins in aqueous solutions. Obtaining low-resolution structure of proteins is still a highly valuable method despite the advances in high-resolution methods such as X-ray diffraction, cryo-EM etc. SAS offers the unique possibility to obtain structural information under conditions close to those of functional assays, i.e. in solution, without different additives, in the mg/mL concentration range. SAS method has a long history, but there are still many uncertainties related to data treatment. We compared 1D SAS profiles of apoferritin obtained by X-ray diffraction (XRD) and SAS methods. It is shown that SAS curves for X-ray diffraction crystallographic structure of apoferritin differ more significantly than it might be expected due to the resolution of the SAS instrument. Extrapolation to infinite dilution (EID) method does not sufficiently exclude dimerization and oligomerization effects and therefore could not guarantee total absence of dimers account in the final SAS curve. In this study, we show that EID SAXS, EID SANS and SEC-SAXS methods give complementary results and when they are used all together, it allows obtaining the most accurate results and high confidence from SAS data analysis of proteins.

Item Type: Article
Erschienen: 2018
Creators: Zabelskii, D. V. ; Vlasov, A. V. ; Ryzhykau, Yu L. ; Murugova, T. N. ; Brennich, M. ; Soloviov, D. V. ; Ivankov, O. I. ; Borshchevskiy, V. I. ; Mishin, A. V. ; Rogachev, A. V. ; Round, A. ; Dencher, N. A. ; Büldt, G. ; Gordeliy, V. I. ; Kuklin, A. I.
Type of entry: Bibliographie
Title: Ambiguities and completeness of SAS data analysis: investigations of apoferritin by SAXS/SANS EID and SEC-SAXS methods
Language: English
Date: 2018
Place of Publication: Bristol
Publisher: IOP Publishing
Journal or Publication Title: Journal of Physics: Conference Series
Volume of the journal: 994
Issue Number: 1
Collation: 11 Seiten
DOI: 10.1088/1742-6596/994/1/012017
Corresponding Links:
Abstract:

The method of small angle scattering (SAS) is widely used in the field of biophysical research of proteins in aqueous solutions. Obtaining low-resolution structure of proteins is still a highly valuable method despite the advances in high-resolution methods such as X-ray diffraction, cryo-EM etc. SAS offers the unique possibility to obtain structural information under conditions close to those of functional assays, i.e. in solution, without different additives, in the mg/mL concentration range. SAS method has a long history, but there are still many uncertainties related to data treatment. We compared 1D SAS profiles of apoferritin obtained by X-ray diffraction (XRD) and SAS methods. It is shown that SAS curves for X-ray diffraction crystallographic structure of apoferritin differ more significantly than it might be expected due to the resolution of the SAS instrument. Extrapolation to infinite dilution (EID) method does not sufficiently exclude dimerization and oligomerization effects and therefore could not guarantee total absence of dimers account in the final SAS curve. In this study, we show that EID SAXS, EID SANS and SEC-SAXS methods give complementary results and when they are used all together, it allows obtaining the most accurate results and high confidence from SAS data analysis of proteins.

Identification Number: Artikel-ID: 012017
Additional Information:

3rd International Summer School and Workshop "Complex and Magnetic Soft Matter Systems: Physico-Mechanical Properties and Structure" 28–30 June 2017, Dubna, Moscow Region, Russian Federation

Classification DDC: 500 Science and mathematics > 530 Physics
500 Science and mathematics > 540 Chemistry
Divisions: 07 Department of Chemistry
07 Department of Chemistry > Clemens-Schöpf-Institut > Fachgebiet Biochemie
07 Department of Chemistry > Clemens-Schöpf-Institut
Date Deposited: 15 May 2024 05:22
Last Modified: 15 May 2024 05:22
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