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Significance The correlation of cryogenic superresolution fluorescence imaging, which features single-molecule sensitivity and specific labelling, with the molecular-scale cellular context of cryogenic electron tomography is a powerful approach for observing the subcellular arrangement of biomolecules. This approach is still in its infancy, and numerous challenges need to be overcome to make this approach routine. This manuscript describes a four-stage workflow using cryogenic single-molecule localizations to annotate cryogenic electron tomography images. The workflow is applied to three different proteins inCaulobacter crescentus and is used to visualize the relative subcellular organization of two proteins, SpmX and PopZ, whose interactions play a key regulatory role in the life cycle ofC. crescentus .

Cryogenic single-molecule fluorescence annotations for electron tomography reveal in situ organization of key proteins in Caulobacter