2023 update of template tables for reporting biomolecular structural modelling of small-angle scattering data

Abstract

In 2017, guidelines were published for reporting structural modelling of small-angle scattering (SAS) data from biomolecules in solution that exemplified best-practice documentation of experiments and analysis. Since then, there has been significant progress in SAS data and model archiving, and the IUCr journal editors announced that the IUCr biology journals will require the deposition of SAS data used in biomolecular structure solution into a public archive, as well as adherence to the 2017 reporting guidelines. In this context, the reporting template tables accompanying the 2017 publication guidelines have been reviewed with a focus on making them both easier to use and more general. With input from the SAS community via the IUCr Commission on SAS and attendees of the triennial 2022 SAS meeting (SAS2022, Campinas, Brazil), an updated reporting template table has been developed that includes standard descriptions for proteins, glycosylated proteins, DNA and RNA, with some reorganization of the data to improve readability and interpretation. In addition, a specialized template has been developed for reporting SAS contrast-variation (SAS-cv) data and models that incorporates the additional reporting requirements from the 2017 guidelines for these more complicated experiments. To demonstrate their utility, examples of reporting with these new templates are provided for a SAS study of a DNA–protein complex and a SAS-cv experiment on a protein complex. The examples demonstrate how the tabulated information promotes transparent reporting that, in combination with the recommended figures and additional information best presented in the main text, enables the reader of the work to readily draw their own conclusions regarding the quality of the data and the validity of the models presented.

Selected advances in small-angle scattering and applications they serve in manufacturing, energy and climate change

“…Coupled with the challenges of higher data rates and the need for rapid data reduction/analysis throughput, both for SAXS and SANS measurements themselves and for paired techniques such as XRD, ND etc., are growing requirements for open data and open publication (cOAlition S, 2020; UNESCO, 2021;International Science Council, 2021) and the need for consistent publication standards. To address these issues, there are growing international efforts, involving major X-ray and neutron facilities, to establish common data formats and standards for metadata (Ko ¨nnecke et al, 2015) that will satisfy FAIR data requirements (Wilkinson et al, 2016), crossplatform reduction and analysis tools, and even research journal publication guidelines (Trewhella et al, 2023). Ultimately, there is a need to establish research data requirements where all tasks -data collection and formatting with metadata for publication, data review and validation, etc.…”

Towards the standardized presentation and publication of small-angle scattering data from biomolecules in solution

“…As a conclusion, the authors point out that it is evident that a single template table cannot account for all the different kinds of SAS experiments involving biomolecules that can be set up or thought of. However, discussions are already ongoing in the SAS community to follow the examples presented here and develop templates for SAS experiments involving nanoparticle/micelle/bicelle-type structures (Trewhella et al, 2023).…”

“…A second objective of Trewhella and coworkers was the creation of a SAS-cv template table, to include the required additional parameters for this type of experiment. Again, Trewhella et al (2023) describe which items have been added and why, with the aim of allowing a broadened applicability, without increasing the workload. To test the relative ease of use and utility of the template, it was populated with data and modelling from a combined SAXS/SANS-cv experiment deposited in SASBDB, of a protein complex consisting of a histidine kinase with bound protein inhibitors that were partially deuterated (Whitten et al, 2007).…”