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
Artikel, Bibliographie
Dies ist die neueste Version dieses Eintrags.
Kurzbeschreibung (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.
| Typ des Eintrags: | Artikel |
|---|---|
| Erschienen: | 2018 |
| Autor(en): | 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. |
| Art des Eintrags: | Bibliographie |
| Titel: | Ambiguities and completeness of SAS data analysis: investigations of apoferritin by SAXS/SANS EID and SEC-SAXS methods |
| Sprache: | Englisch |
| Publikationsjahr: | 2018 |
| Ort: | Bristol |
| Verlag: | IOP Publishing |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | Journal of Physics: Conference Series |
| Jahrgang/Volume einer Zeitschrift: | 994 |
| (Heft-)Nummer: | 1 |
| Kollation: | 11 Seiten |
| DOI: | 10.1088/1742-6596/994/1/012017 |
| Zugehörige Links: | |
| Kurzbeschreibung (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. |
| ID-Nummer: | Artikel-ID: 012017 |
| Zusätzliche Informationen: | 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 |
| Sachgruppe der Dewey Dezimalklassifikatin (DDC): | 500 Naturwissenschaften und Mathematik > 530 Physik 500 Naturwissenschaften und Mathematik > 540 Chemie |
| Fachbereich(e)/-gebiet(e): | 07 Fachbereich Chemie 07 Fachbereich Chemie > Clemens-Schöpf-Institut > Fachgebiet Biochemie 07 Fachbereich Chemie > Clemens-Schöpf-Institut |
| Hinterlegungsdatum: | 15 Mai 2024 05:22 |
| Letzte Änderung: | 15 Mai 2024 05:22 |
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Ambiguities and completeness of SAS data analysis: investigations of apoferritin by SAXS/SANS EID and SEC-SAXS methods. (deposited 14 Mai 2024 09:50)
- Ambiguities and completeness of SAS data analysis: investigations of apoferritin by SAXS/SANS EID and SEC-SAXS methods. (deposited 15 Mai 2024 05:22) [Gegenwärtig angezeigt]
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