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The full understanding of cellular functions requires information aboutprotein numbers for various biomolecular assemblies and their dynamics, whichcan be partly accessed by super-resolution fluorescence microscopy. Yet, manyprotein assemblies and cellular structures remain below the accessibleresolution on the order of tens of nanometers thereby evading directobservation of processes, like self-association or oligomerization, that arecrucial for many cellular functions. Over the recent years, several approacheshave been developed addressing concentrations and copy numbers of biomoleculesin cellular samples for specific applications. This has been achieved by newlabeling strategies and improved sample preparation as well as advancements insuperresolution and single-molecule fluorescence microscopy. So far, none ofthe methods has reached a level of general and versatile usability due toindividual advantages and limitations. In this article, important requirementsof an ideal quantitative microscopy approach of general usability are outlinedand discussed in the context of existing methods including sample preparationand labeling quality which are essential for the robustness and reliability ofthe methods and future applications in cell biology.

Photons in - numbers out: Perspectives in quantitative fluorescence microscopy for in situ protein counting