Abstract
Single-Molecule Localisation Microscopy (SMLM) allows the quantitative mapping of molecules at high resolution. However, understanding the non-random interaction of proteins requires the identification of more complex patterns than those typified by standard clustering tools. Here we introduce SuperStructure, a parameter-free algorithm to quantify structures made of inter-connected clusters, such as protein gels. SuperStructure works without a priori assumptions and is thus an ideal methodology for standardised analysis of SMLM data.
Competing Interest Statement
The authors have declared no competing interest.
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