SAXS fitting data and atomic structures for all models described in the manuscript "Plasticity and co-factor dependent structural changes of the RecA nucleoprotein filament studied by SAXS measurements and molecular modeling", by Inaba-Inoue and co-authors. This data concerns the solution structures of two filament forms resulting from the self-assembly of the RecA protein, active in the homologous recombination process in prokaryotes. The extended form is obtained in the presence of ATP and magnesium, the compressed form is obtained in the absence of either ATP or magnesium. The data is distributed in two .zip files, SAXS_data.zip and Models.zip. SAXS_data contains foXS output fitting data obtained for each of the models discussed in the manuscript, relative to experimental SAXS profiles. Models contains the structures at atomic resolution of all models discussed in the manuscript (.pdb format) The data in each repository is distributed in two directories: Extended and Compressed. The data in the Extended directory concerns the extended form of the filament: Models pdb files (atomic coordinates) named after Table SI_1 of the manuscript SAXS_data fitting data (.fit) ADP/ATP_model_SAXS_profiles: fit over the whole range of q values Files are named after Table SI_1 of the manuscript 003_015: fit over q values in the interval [0.03;0.15] /Å Files are named after the originally constructed models graphical representation of the fit between the predicted and experimental SAXS profiles output by the foXS web server (https://salilab.org/foxs; Schneidman-Duhovny, 2016) (.png and .pdf) compressed/extended_name_correspondence.txt: displays the correspondence between the model names in the article and the names of the originally constructed models (text file) file_description.txt (text file) FoXS Reference Schneidman-Duhovny, D.; Hammel, M.; Tainer, J.A.; Sali, A. FoXS, FoXSDock and MultiFoXS: Single-state and multi-state structural modeling of proteins and their complexes based on SAXS profiles. Nucleic Acids Res 2016, 44, W424–9.