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Single-molecule and superresolution imaging in live bacteria cells Biteen JS; Moerner WECold Spring Harb Perspect Biol 2010[Mar]; 2 (3): a000448Single-molecule imaging enables biophysical measurements devoid of ensemble averaging, gives enhanced spatial resolution beyond the diffraction limit, and permits superresolution reconstructions. Here, single-molecule and superresolution imaging are applied to the study of proteins in live Caulobacter crescentus cells to illustrate the power of these methods in bacterial imaging. Based on these techniques, the diffusion coefficient and dynamics of the histidine protein kinase PleC, the localization behavior of the polar protein PopZ, and the treadmilling behavior and protein superstructure of the structural protein MreB are investigated with sub-40-nm spatial resolution, all in live cells.|*Bacterial Physiological Phenomena[MESH]|Bacterial Proteins/chemistry[MESH]|Biophysics/methods[MESH]|Caulobacter crescentus/*metabolism[MESH]|Cell Cycle[MESH]|Cryoelectron Microscopy/methods[MESH]|Cytoplasm/metabolism[MESH]|Diffusion[MESH]|Escherichia coli Proteins/metabolism[MESH]|Histidine Kinase[MESH]|Luminescent Proteins/chemistry[MESH]|Microscopy, Fluorescence/methods[MESH]|Models, Biological[MESH]|Protein Kinases/metabolism[MESH] |
