Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Nelly R. Hajizadeh"'
Publikováno v:
Scientific Reports, Vol 8, Iss 1, Pp 1-13 (2018)
Abstract Molecular mass (MM) is one of the key structural parameters obtained by small-angle X-ray scattering (SAXS) of proteins in solution and is used to assess the sample quality, oligomeric composition and to guide subsequent structural modelling
Externí odkaz:
https://doaj.org/article/64ea8341bdef4605ab3728253d908a36
Autor:
Karen Manalastas-Cantos, Daniel Franke, Alexey Kikhney, Dmitri I. Svergun, Andrey Yu. Gruzinov, Martin A. Schroer, Florian Schulz, Nelly R. Hajizadeh, Clement E. Blanchet
Publikováno v:
Journal of synchrotron radiation 28(3), 812-823 (2021). doi:10.1107/S1600577521003404
Journal of Synchrotron Radiation
Journal of Synchrotron Radiation
Journal of synchrotron radiation 28(3), 812-823 (2021). doi:10.1107/S1600577521003404
Small-angle X-ray scattering (SAXS) is an established method for studyingnanostructured systems and in particular biological macromolecules in solution.To obta
Small-angle X-ray scattering (SAXS) is an established method for studyingnanostructured systems and in particular biological macromolecules in solution.To obta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::20c53daa91396e777c2e5bccbe5c4ca3
https://doi.org/10.1107/s1600577521003404
https://doi.org/10.1107/s1600577521003404
Autor:
Cy M. Jeffries, Clemente R. Borges, Petr V. Konarev, Nelly R. Hajizadeh, Dmitry S. Molodenskiy, Haydyn D. T. Mertens, Dmitri I. Svergun, Daniel Franke, Andrey Yu. Gruzinov, Maxim V. Petoukhov, Alexey Kikhney, Karen Manalastas-Cantos, Alejandro Panjkovich
Publikováno v:
Journal of Applied Crystallography
The ATSAS software suite encompasses a number of programs for the processing, visualization, analysis and modelling of small‐angle scattering data, with a focus on the data measured from biological macromolecules. Here, new developments in the ATSA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb869db85e4fd089c57967b9bb02bcd6
Publikováno v:
Journal of Applied Crystallography
Journal of applied crystallography 53(2), 536-539 (2020). doi:10.1107/S1600576720000527
Journal of applied crystallography 53(2), 536-539 (2020). doi:10.1107/S1600576720000527
Journal of applied crystallography 53(2), 536 - 539 (2020). doi:10.1107/S1600576720000527
This article presents IMSIM, an application to simulate two-dimensional small-angle X-ray scattering patterns and, further, one-dimensional profiles from b
This article presents IMSIM, an application to simulate two-dimensional small-angle X-ray scattering patterns and, further, one-dimensional profiles from b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::adaa836e02df492c05ed949269900f7f
Publikováno v:
Journal of Synchrotron Radiation
Journal of synchrotron radiation 25(3), 906-914 (2018). doi:10.1107/S1600577518005398
Journal of synchrotron radiation 25(3), 906-914 (2018). doi:10.1107/S1600577518005398
Journal of synchrotron radiation 25(3), 906 - 914 (2018). doi:10.1107/S1600577518005398
The versatility of small-angle X-ray scattering (SAXS) as a structural biology method is apparent by its compatibility with many experimental set-ups. Most a
The versatility of small-angle X-ray scattering (SAXS) as a structural biology method is apparent by its compatibility with many experimental set-ups. Most a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe3f99506de922ba81e2988712543ee6
Publikováno v:
Acta Crystallographica Section D: Biological Crystallography
The biophysical characterization of protein–ligand interactions in solution using techniques such as thermal shift assay, or on surfaces using, for example, dual polarization interferometry, plays an increasingly important role in complementing cry
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d7dd237d61cf73066fef36672d163a0
https://doi.org/10.1107/s1399004714016617
https://doi.org/10.1107/s1399004714016617
Publikováno v:
Scientific Reports
Scientific Reports, Vol 8, Iss 1, Pp 1-13 (2018)
Scientific Reports, Vol 8, Iss 1, Pp 1-13 (2018)
Molecular mass (MM) is one of the key structural parameters obtained by small-angle X-ray scattering (SAXS) of proteins in solution and is used to assess the sample quality, oligomeric composition and to guide subsequent structural modelling. Concent
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de0aba8183560a6b01cbecc59a7c96b9
https://pubmed.ncbi.nlm.nih.gov/29739979
https://pubmed.ncbi.nlm.nih.gov/29739979
Autor:
Anne T. Tuukkanen, Cy M. Jeffries, Alejandro Panjkovich, Peter V. Konarev, J.M. Franklin, Dmitri I. Svergun, Alexey Kikhney, Haydyn D. T. Mertens, Nelly R. Hajizadeh, Daniel Franke, Maxim V. Petoukhov
Publikováno v:
Journal of Applied Crystallography
Developments and improvements of the ATSAS software suite (versions 2.5–2.8) for analysis of small-angle scattering data of biological macromolecules or nanoparticles are described.
ATSAS is a comprehensive software suite for the analysis of s
ATSAS is a comprehensive software suite for the analysis of s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4cab1e2e21522527b4ab341bb9e3d23b
Autor:
Joanna Pieprzyk, Petr Skopintsev, Nelly R. Hajizadeh, Dmitri I. Svergun, Christian Löw, Ali Flayhan
Publikováno v:
Structure
The scaffolding protein PDZK1 has been associated with the regulation of membrane transporters. It contains four conserved PDZ domains, which typically recognize a 3-5-residue long motif at the C terminus of the binding partner. The atomic structures
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::79a0cbac48a2e7fa711a69b99eeeb7ac
https://doi.org/10.1016/j.str.2018.07.016
https://doi.org/10.1016/j.str.2018.07.016
Publikováno v:
Acta Crystallographica Section A Foundations and Advances. 73:C656-C656
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f352edd190b21a12ae41364c017145b4
https://doi.org/10.1107/s2053273317089173
https://doi.org/10.1107/s2053273317089173