Advanced sample environments and sample requirements for biological SAXS

BioXTAS RAW 2: new developments for a free open-source program for small-angle scattering data reduction and analysis

“…SAS provides information on the solution state of macromolecules and complexes, including, but not limited to, size and molecular weight (MW), flexibility, degree of folding, and overall shape (Trewhella, 2022;Da Vela & Svergun, 2020;Brosey & Tainer, 2019;Meisburger et al, 2017;Jacques & Trewhella, 2010;. The growing popularity of SAS as part of the structural biology toolbox has many contributing factors: expanding data-collection capabilities for more challenging systems, including the increasing number of hyphenated techniques like size-exclusion or ion-exchange chromatography coupled to SAXS (SEC-SAXS and IEC-SAXS) (Graewert & Svergun, 2022;Pe ´rez et al, 2022); increasing automation of data collection and analysis to make the technique more accessible for new users (Tully et al, 2023;Rosenberg et al, 2022;Lazo et al, 2021); and an increasing awareness that SAS is highly complementary to other structural and biophysical techniques such as X-ray crystallography (MX), nuclear magnetic resonance, cryo-electron microscopy (cryo-EM), and multi-angle (also called static) and dynamic light scattering (Trewhella, 2022;Brosey & Tainer, 2019;Grishaev, 2017). Additionally, SAS has proven an invaluable tool for studying intrinsically disordered proteins and liquidliquid phase separating systems, which are not readily amenable to common high-resolution structural techniques such as MX and cryo-EM (Lenton et al, 2022;Martin et al, 2020;Sagar et al, 2020;Riback et al, 2017;Kikhney & Svergun, 2015).…”

BioXTAS RAW 2: new developments for a free open-source program for small angle scattering data reduction and analysis

“…SAS provides information on the solution state of macromolecules and complexes, including, but not limited to, size and molecular weight, flexibility, degree of folding, and overall shape (Trewhella, 2022; Da Vela & Svergun, 2020; Brosey & Tainer, 2019; Meisburger et al ., 2017; Jacques & Trewhella, 2010; Svergun & Koch, 2003). The growing popularity of SAS as part of the structural biology toolbox has many contributing factors: expanding data collection capabilities for more challenging systems, including the increasing number of hyphenated techniques like size exclusion or ion exchange chromatography coupled to SAXS (SEC-SAXS and IEC-SAXS) (Graewert & Svergun, 2022; Pérez et al ., 2022); increasing automation of data collection and analysis to make the technique more accessible for new users (Tully et al ., 2023; Rosenberg et al ., 2022; Lazo et al ., 2021); and an increasing awareness that SAS is highly complementary to other structural and biophysical techniques such as X-ray crystallography (MX), nuclear magnetic resonance (NMR), cryo-electron microscopy (cryoEM), and multi-angle (also called static) and dynamic light scattering (Trewhella, 2022; Brosey & Tainer, 2019; Grishaev, 2017). Additionally, SAS has proven an invaluable tool for studying intrinsically disordered proteins and liquid-liquid phase separating systems, which are not readily amenable to common high-resolution structural techniques such as MX and cryoEM (Lenton et al ., 2022; Martin, Hopkins et al ., 2021; Martin et al ., 2020; Sagar et al ., 2020; Riback et al ., 2017; Kikhney & Svergun, 2015).…”