Curated repository for small angle scattering data and models


SASBDB currently contains:


4844

experimental data sets

6041

models
554 experimental data sets on hold
760 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:

SASDVE4 – Shwachman-Bodian-Diamond syndrome protein (SBDS) - I167T mutant

Ribosome maturation protein SBDS (I167T) experimental SAS data
MULTIFOXS model
Sample: Ribosome maturation protein SBDS (I167T) monomer, 29 kDa Homo sapiens protein
Buffer: 50 mM Tris pH 8.0, 10% glycerol, 300 mM NaCl, 5 mM MgCl2., pH:
Experiment: SAXS data collected at EMBL P12, PETRA III on 2022 Apr 6
Structural Implications of Missense Point Mutations in Shwachman–Bodian–Diamond Syndrome Protein (SBDS): A Combined SAXS/MD Investigation ACS Omega (2025)
Mattiotti G, Nanna V, Giulini M, Alberga D, Mangiatordi G, Sánchez-Puig N, Saviano M, Tubiana L, Potestio R, Lattanzi G, Siliqi D
RgGuinier 2.9 nm
Dmax 10.5 nm
VolumePorod 44 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.