Method-specific Validation Task Forces have been convened to collect recommendations and develop consensus on additional validation that should be performed, and to identify software applications to perform validation tasks.
The first meeting of the Small Angle Scattering (SAS) Task Force was held July 12-13, 2012 at the Center for Integrative Proteomics Research at Rutgers University in Piscataway, NJ.
Their report has now been published:
"Report of the wwPDB Small-Angle Scattering Task Force: Data Requirements for Biomolecular Modeling and the PDB Structure" Jill Trewhella, Wayne A. Hendrickson, Gerard J. Kleywegt, Andrej Sali, Mamoru Sato, Torsten Schwede, Dmitri I. Svergun, John A. Tainer, John Westbrook and Helen M. Berman (2013) Structure 21: 875-881 [ doi:10.1016/j.str.2013.04.020 ]
A second meeting was held May 12-14, 2014 at Rutgers. Participants included Jill Trewhella (Chair, University of Sydney), Torsten Schwede (University of Basel), Shuji Akiyama (Research Center of Integrative Molecular Systems (CIMoS), Japan), Dmitri Svergun (EMBL-Hamburg), Wayne Hendrickson (Columbia University), John A. Tainer (The Scripps Research Institute), and Andrej Sali (University of California at San Francisco) and wwPDB Representatives Helen Berman (RCSB PDB), Stephen Burley (RCSB PDB), Gerard Kleywegt (PDBe), John Westbrook (RCSB PDB), and Cathy Lawson (RCSB PDB)
An outcome of a project aimed to test and benchmark different approaches for modelling SAS profiles from PDB coordinates has been published:
A round-robin approach provides a detailed assessment of biomolecular small-angle scattering data reproducibility and yields consensus curves for benchmarking
Trewhella, J., Vachette, P., Bierma, J., Blanchet, C., Brookes, E., Chakravarthy, S., Chatzimagas, L., Cleveland, T. E., Cowieson, N., Crossett, B., Duff, A. P., Franke, D., Gabel, F., Gillilan, R. E., Graewert, M., Grishaev, A., Guss, J. M., Hammel, M., Hopkins, J., Huang, Q., Hub, J. S., Hura, G. L., Irving, T. C., Jeffries, C. M., Jeong, C., Kirby, N., Krueger, S., Martel, A., Matsui, T., Li, N., Perez, J., Porcar, L., Prange, T., Rajkovic, I., Rocco, M., Rosenberg, D. J., Ryan, T. M., Seifert, S., Sekiguchi, H., Svergun, D., Teixeira, S., Thureau, A., Weiss, T. M., Whitten, A. E., Wood, K. & Zuo, X.
(2022) Acta Cryst. D78: 1315-1336 doi: 10.1107/S2059798322009184
In total, 171 SAXS and 76 SANS measurements for five proteins (ribonuclease A, lysozyme, xylanase, urate oxidase and xylose isomerase) were collected and analysed centrally. In the process, new methods for data comparing and merging were developed. The data produced for this effort, has been deposited in the SAS Biological Data Bank (SASBDB) as consensus data along with the contributing individual data sets.
A chapter describing the work done to establish the 2017 publication guidelines for biomolecular SAS, the establishment of the SASBDB, and the evolution and outcomes of the benchmarking project has been published:
Chapter One - Data quality assurance, model validation, and data sharing for biomolecular structures from small-angle scattering
(2023) Methods in Enzymology 678: 1-22 doi: 10.1016/bs.mie.2022.11.002
An updated template reporting table for biomolecular SAXS data has been published:
2023 update of template tables for reporting biomolecular structural modelling of small-angle scattering data
J. Trewhella, C. M. Jeffries and A. E. Whitten (2023) Acta Cryst. D79: 122-132 doi: 10.1107/S2059798322012141