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Coordinate transformation based cryo-correlative methods for electron tomography and focused ion beam milling

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Fukuda,  Yoshiyuki
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Schrod,  Nikolas
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Schaffer,  Miroslava
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Feng,  Li Rebekah
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Baumeister,  Wolfgang
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Lucic,  Vladan
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Fukuda, Y., Schrod, N., Schaffer, M., Feng, L. R., Baumeister, W., & Lucic, V. (2014). Coordinate transformation based cryo-correlative methods for electron tomography and focused ion beam milling. ULTRAMICROSCOPY, 143(SI: Correlative Microscopy), 15-23. doi:10.1016/j.ultramic.2013.11.008.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0019-CE29-7
Abstract
Correlative microscopy allows imaging of the same feature over multiple length scales, combining light microscopy with high resolution information provided by electron microscopy. We demonstrate two procedures for coordinate transformation based correlative microscopy of vitrified biological samples applicable to different imaging modes. The first procedure aims at navigating cryo-electron tomography to cellular regions identified by fluorescent labels. The second procedure, allowing navigation of focused ion beam milling to fluorescently labeled molecules, is based on the introduction of an intermediate scanning electron microscopy imaging step to overcome the large difference between cryo-light microscopy and focused ion beam imaging modes. These methods make it possible to image fluorescently labeled macromolecular complexes in their natural environments by cryo-electron tomography, while minimizing exposure to the electron beam during the search for features of interest. (C) 2013 Elsevier B.V. All rights reserved.