Last time updated: February 2024
The eSPC platform (spc.embl-hamburg.de) is a collection of programs designed to analyze biophysical data using different techniques. The table below shows the tools available along with their purpose:
| Tool | Purpose | Technique |
|---|---|---|
| MoltenProt | Protein stability | Differential scanning fluorimetry |
| FoldAffinity | Binding affinity | Differential scanning fluorimetry |
| ThermoAffinity | Binding affinity | Microscale thermophoresis / fluorescence quenching |
| PhotoMol | Sample size, oligomerization and homogeneity | Mass photometry |
| Raynals | Sample size and homogeneity | Single-angle dynamic light scattering |
| ChiraKit | Protein stability, secondary structure, binding | Circular dichroism |
To install all or some of the eSPC platform tools, please refer to the 'installation_guide.md' document.
Developers: Osvaldo Burastero, Stephan Niebling, Clemente Borges and Andrea D'Amato
Project Leader: Maria Garcia Alai
If you have any questions or feedback regarding the eSPC platform, or you want to provide your own version of the eSPC platform on a different host, please feel free to contact us via email:
oburastero@gmail.com, stephan.niebling@embl-hamburg.de, m.garcia@embl-hamburg.de, spc@embl-hamburg.de
Burastero, Osvaldo, et al. "Raynals, an online tool for the analysis of dynamic light scattering." Acta Crystallographica Section D: Structural Biology 79.8 (2023).
Niebling, Stephan, et al. "Biophysical Screening Pipeline for Cryo-EM Grid Preparation of Membrane Proteins." Frontiers in Molecular Biosciences (2022): 535.
Burastero, Osvaldo, et al. "eSPC: an online data-analysis platform for molecular biophysics." Acta Crystallographica Section D: Structural Biology 77.10 (2021): 1241-1250.
Niebling, Stephan, et al. "FoldAffinity: binding affinities from nDSF experiments." Scientific Reports 11.1 (2021): 9572.