The SAXS solution structure of RF1 differs from its crystal structure and is similar to its ribosome bound cryo-EM structure.
Bente Vestergaard,Suparna Sanyal,Manfred Roessle,Liliana Mora,Richard H. Buckingham,Jette S. Kastrup,Michael Gajhede,Dmitri I. Svergun,Måns Ehrenberg +8 more
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Small-angle X-ray scattering data from E. coli RF1 and from a functionally active truncated RF1 derivative obviate the need for assuming large conformational changes in RFs during termination.About:
This article is published in Molecular Cell.The article was published on 2005-12-22 and is currently open access. It has received 103 citations till now.read more
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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.
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X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution.
TL;DR: In this article, a review of the use of small angle X-ray scattering (SAXS) for modeling macromolecular folding, unfolding, aggregation, extended conformations, flexibly linked domains, shape, conformation, and assembly state in solution, albeit at the lower resolution range of about 50 A to 10 A resolution, is presented.
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Structural characterization of proteins and complexes using small-angle X-ray solution scattering.
TL;DR: Main approaches to the characterization of proteins and protein complexes using SAXS are reviewed, and main tools for the analysis of proteins in solution are presented, and the impact that these tools have made in modern structural biology is discussed.
Journal ArticleDOI
Structure and flexibility within proteins as identified through small angle X-ray scattering.
TL;DR: An analysis tool is described using relatively inexpensive small angle X-ray scattering (SAXS) measurements to identify flexibility and validate a constructed minimal ensemble of models, which represent highly populated conformations in solution.
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Small-angle scattering for structural biology—Expanding the frontier while avoiding the pitfalls
David A. Jacques,Jill Trewhella +1 more
TL;DR: This review is intended to provide a road map through the small‐angle scattering experiment, while also providing a set of guidelines for the critical evaluation of scattering data.
References
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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
Axel T. Brunger,Axel T. Brunger,Paul D. Adams,G M Clore,W. L. DeLano,Piet Gros,R.W. Grosse-Kunstleve,R.W. Grosse-Kunstleve,Jiansheng Jiang,J. Kuszewski,Michael Nilges,Navraj S. Pannu,Randy J. Read,Luke M. Rice,Thomas Simonson,Gregory L. Warren +15 more
TL;DR: The Crystallography & NMR System (CNS) as mentioned in this paper is a software suite for macromolecular structure determination by X-ray crystallography or solution nuclear magnetic resonance (NMR) spectroscopy.
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Determination of the regularization parameter in indirect-transform methods using perceptual criteria
TL;DR: In this paper, a method is proposed for the determination of the optimum value of the regularization parameter (Lagrange multiplier) when applying indirect transform techniques in small-angle scattering data analysis.
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CRYSOL : a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
TL;DR: In this paper, a program for evaluating the solution scattering from macromolecules with known atomic structure is presented, which uses multipole expansion for fast calculation of the spherically averaged scattering pattern and takes into account the hydration shell.
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PRIMUS: a Windows PC-based system for small-angle scattering data analysis
Petr V. Konarev,Petr V. Konarev,Vladimir Volkov,Vladimir Volkov,Anna Sokolova,Anna Sokolova,Michel H. J. Koch,Dmitri I. Svergun,Dmitri I. Svergun +8 more
TL;DR: A program suite for one-dimensional small-angle scattering data processing running on IBM-compatible PCs under Windows 9x/NT/2000/XP is presented and PRIMUS enables model-independent singular value decomposition or linear fitting if the scattering from the components is known.