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Related Experiment Video

Updated: Feb 24, 2026

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering

Published on: November 5, 2018

ATSAS 2.8: a comprehensive data analysis suite for small-angle scattering from macromolecular solutions.

D Franke¹, M V Petoukhov^1,2,3, P V Konarev^2,4

¹European Molecular Biology Laboratory, Hamburg Outstation, Notkestrasse 85, D-22607 Hamburg, Germany.

Journal of Applied Crystallography

|August 16, 2017

Summary

This summary is machine-generated.

The ATSAS software suite has been updated for analyzing biological macromolecule and nanoparticle scattering data. New features enhance data assessment, ab initio modeling, and hybrid model construction for structural biology research.

Keywords:

ATSAS biological macromolecules data analysis small-angle scattering structural modelling

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Last Updated: Feb 24, 2026

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering

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Published on: November 5, 2018

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Small and Wide Angle X-Ray Scattering Studies of Biological Macromolecules in Solution

Small and Wide Angle X-Ray Scattering Studies of Biological Macromolecules in Solution

Published on: January 8, 2013

Area of Science:

Structural Biology
Biophysics
Computational Biology

Background:

Small-angle scattering (SAS) is crucial for determining the structure of biological macromolecules and nanoparticles in solution.
Existing software suites require continuous development to incorporate new analytical methods and improve user experience.

Purpose of the Study:

To summarize advancements in the ATSAS software suite during the 2.5-2.8 release series.
To highlight new tools for enhanced analysis of small-angle scattering data and model building.

Main Methods:

The ATSAS software suite integrates various computational methods for SAS data analysis.
New tools include AMBIMETER for reconstruction ambiguity, DATCLASS for shape classification, SASRES for resolution estimation, and CHROMIXS for chromatography analysis.
Further developments include SHANUM for data range evaluation, SREFLEX for model refinement, SUPALM for model superposition, and SASPy for PyMOL integration.

Main Results:

The ATSAS 2.8 release incorporates significant improvements and new functionalities.
New tools enable more robust assessment of experimental data quality and model reliability.
Enhanced capabilities for hybrid model construction using complementary structural data are now available.

Conclusions:

The ATSAS software suite provides a comprehensive platform for SAS data analysis.
The latest release offers advanced tools for structural biology, facilitating more accurate and efficient macromolecular and nanoparticle structure determination.
ATSAS 2.8 is freely available for academic users.