Correlative three-dimensional super-resolution and block face electron microscopy of whole vitreously frozen cells
David P. Hoffman,
C. Shan Xu,
Kirby R. Campbell,
Daniel E. Milkie,
H. Amalia Pasolli,
Daniel R. Stabley,
David J. Solecki,
Harald F. Hess
Posted 18 Sep 2019
bioRxiv DOI: 10.1101/773986 (published DOI: 10.1126/science.aaz5357)
Posted 18 Sep 2019
Living cells function through the spatial compartmentalization of thousands of distinct proteins serving a multitude of diverse biochemical needs. Correlative super-resolution (SR) fluorescence and electron microscopy (EM) has emerged as a pathway to directly view nanoscale protein relationships to the underlying global ultrastructure, but has traditionally suffered from tradeoffs of structure preservation, fluorescence retention, resolution, and field of view. We developed a platform for three-dimensional correlative cryogenic SR and focused ion beam milled block-face EM across entire vitreously frozen cells that addresses these issues by preserving native ultrastructure and enabling independent SR and EM workflow optimization. Application to a variety of biological systems revealed a number of unexpected protein-ultrastructure relationships and underscored the value of a comprehensive multimodal view of ultrastructural variability across whole cells.
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