Curated repository for small angle scattering data and models


SASBDB currently contains:


5181

experimental data sets

6395

models
599 experimental data sets on hold
936 models on hold

Small angle scattering (SAS) of X-ray and neutrons provides structural information on biological macromolecules in solution at a resolution of 1-2 nm.
SASBDB is a fully searchable curated repository of freely accessible and downloadable experimental data, which are deposited together with the relevant experimental conditions, sample details, derived models and their fits to the data.

Recent depositions:

SASDY97 – Alkaline phosphatase (ALP) under vis

Wild Alkaline Phosphatase under vis experimental SAS data
PYMOL model
Sample: Wild Alkaline Phosphatase under vis dimer, 97 kDa Escherichia coli protein
Buffer: 25 mM Tris, 100 mM NaCl, 2 mM TCEP, 3% (w/v) glycerol, pH: 7.5
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2024 Dec 23
Single-engineered-residue solvation perturbations regulate global protein architecture and function. Nat Commun (2026)
Liu Y, Zhai J, Cao S, Guo H, Zhang H, Song B, Guo J, Men D, He X, Li D
RgGuinier 2.8 nm
Dmax 9.0 nm
VolumePorod 75 nm3

Browse the contents according to:

Organism
Macromolecule type
Model type
Dissemination type
To cite SASBDB refer to: Kikhney AG, Borges CR, Molodenskiy DS, Jeffries CM, Svergun DI (2020) SASBDB: Towards an automatically curated and validated repository for biological scattering data. Protein Science 29(1); 66-75.