The current challenges of structural biophysics include determining the structure of large self-assembled complexes, resolving the structure of ensembles of complex structures and their mass fraction, and unraveling the dynamic pathways and mechanisms leading to the formation of complex structures from their subunits. Modern synchrotron solution X-ray scattering data enable simultaneous high-spatial and high-temporal structural data required to address the current challenges of structural biophysics. These data are complementary to crystallography, NMR, and cryo-TEM data. However, the analysis of solution scattering data is challenging; hence many different analysis tools, listed in the SAS Portal (http://smallangle.org/), were developed. In this review, we start by briefly summarizing classical X-ray scattering analyses providing insight into fundamental structural and interaction parameters. We then describe recent developments, integrating simulations, theory, and advanced X-ray scattering modeling, providing unique insights into the structure, energetics, and dynamics of self-assembled complexes. The structural information is essential for understanding the underlying physical chemistry principles leading to self-assembled supramolecular architectures and computational structural refinement.
Bibliographical noteFunding Information:
We acknowledge the European Synchrotron Radiation Facility (ESRF) beamline ID02 (T. Narayanan and his team), Desy synchrotron at Hamburg, beamline P12 (D. Svergun and his team), and Soleil synchrotron, Swing beamline (J. Perez and his team), for provision of synchrotron radiation facilities and for assistance in using them. This project was supported by the Israel Science Foundation and the Israel Ministry of Science. We thank the Safra, Wolfson, and Rudin Foundations for supporting our laboratory.
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- Time-resolved SAXS