M
Maxim V. Petoukhov
Researcher at Russian Academy of Sciences
Publications - 86
Citations - 10583
Maxim V. Petoukhov is an academic researcher from Russian Academy of Sciences. The author has contributed to research in topics: Scattering & Protein structure. The author has an hindex of 34, co-authored 81 publications receiving 9287 citations. Previous affiliations of Maxim V. Petoukhov include Moscow State University & European Bioinformatics Institute.
Papers
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Journal ArticleDOI
New developments in the ATSAS program package for small-angle scattering data analysis
Maxim V. Petoukhov,Daniel Franke,Alexander V. Shkumatov,Giancarlo Tria,Alexey Kikhney,Michal J. Gajda,Christian Gorba,Haydyn D. T. Mertens,Petr V. Konarev,Dmitri I. Svergun +9 more
TL;DR: The paper presents new developments and amendments to the ATSAS package (version 2.4) for processing and analysis of isotropic small-angle scattering data.
Journal ArticleDOI
Determination of domain structure of proteins from X-ray solution scattering.
TL;DR: The new method substantially improves the resolution and reliability of models derived from scattering data and makes solution scattering a useful technique in large-scale structural characterization of proteins.
Journal ArticleDOI
ATSAS 2.8: a comprehensive data analysis suite for small-angle scattering from macromolecular solutions
Daniel Franke,Maxim V. Petoukhov,Maxim V. Petoukhov,Peter V. Konarev,Peter V. Konarev,Alejandro Panjkovich,Anne T. Tuukkanen,Haydyn D. T. Mertens,Alexey Kikhney,Nelly R. Hajizadeh,J.M. Franklin,Cy M. Jeffries,Dmitri I. Svergun +12 more
TL;DR: Developments and improvements of the ATSAS software suite for analysis of small-angle scattering data of biological macromolecules or nanoparticles are described.
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Structural Characterization of Flexible Proteins Using Small-Angle X-ray Scattering
TL;DR: A new approach, ensemble optimization method (EOM), is proposed to quantitatively characterize flexible proteins in solution using small-angle X-ray scattering (SAXS), and is able to distinguish between rigid and flexible proteins and to directly assess the interdomain contacts.
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Global rigid body modeling of macromolecular complexes against small-angle scattering data
TL;DR: New methods to automatically build models of macromolecular complexes from high-resolution structures or homology models of their subunits or domains against x-ray or neutron small-angle scattering data are presented and allow one to construct interconnected models without steric clashes.