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Boris preprint DOI: https://doi.org/10.1101/2024.06.18.599606; this version posted June 20, 2024. The copyright holder for this preprint (which was not certified by peer review) is the author/funder,
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01
Prepare your sample by flash-freezing it in liquid ethane to preserve its native state.
02
Place the frozen sample in a cryo-electron microscope for imaging.
03
Collect a series of 2D projection images at various angles.
04
Use software to align and combine the 2D images into a 3D reconstruction.
05
Refine the 3D structure by applying image processing techniques to enhance the resolution.
06
Analyze the resulting tomograms to extract relevant biological information.

Who needs cryo-electron tomography reveals the?

01
Structural biologists studying macromolecular complexes.
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Researchers investigating disease mechanisms at the cellular level.
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Pharmaceutical companies developing drugs targeting specific proteins.
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Academics conducting advanced studies in cell biology and biochemistry.
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Cryo-electron tomography reveals the three-dimensional structure of biological samples at nanoscale resolution, allowing researchers to visualize cellular components in their native state.
Researchers and scientists involved in structural biology and microscopy studies may be required to file results or findings related to cryo-electron tomography.
To fill out cryo-electron tomography documentation, researchers must accurately record experimental conditions, sample details, and any relevant data derived from the imaging process.
The purpose of cryo-electron tomography is to obtain detailed insights into the architecture of biological specimens without the need for dehydration or staining, preserving their natural state.
Information that must be reported includes sample preparation methods, imaging parameters, data processing techniques, and findings related to the 3D structures observed.
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