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The eSPC platform

Last time updated: February 2026

Introduction

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
KinGenie Binding kinetics Biolayer interferometry, surface plasmon resonance

Installation

To install all or some of the eSPC platform tools, please refer to the 'installation_guide.md' document.

Team

Developers: Osvaldo Burastero, Florian Vögele
Previous developers: Stephan Niebling, Clemente Borges and Andrea D'Amato
Project leader: Maria Marta Garcia Alai

Contact

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:

spc@embl-hamburg.de

Main references

Burastero, Osvaldo, et al. "ChiraKit: an online tool for the analysis of circular dichroism spectroscopy data." Nucleic Acids Research 53.W1 (2025): W158-W168.

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.

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