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Related Concept Videos

Cryo-electron Microscopy01:28

Cryo-electron Microscopy

Conventional electron microscopy (EM) involves dehydration, fixation, and staining of biological samples, which distorts the native state of biological molecules and results in several artifacts. Also, the high-energy electron beam damages the sample and makes it difficult to obtain high-resolution images. These issues can be addressed using cryo-EM, which uses frozen samples and gentler electron beams. The technique was developed by Jacques Dubochet, Joachim Frank, and Richard Henderson, for...
Studying the Cytoskeleton01:17

Studying the Cytoskeleton

The cytoskeletal architecture can be studied using different microscopic and biochemical techniques. Electron microscopy was instrumental in discovering the cytoskeletal architecture around the 1960s, which allowed obtaining structural information at a high-resolution level. However, the sample preparation procedure often limits this ability in biological samples. Several protocols have been developed over the years to optimize sample preparation. In one of the protocols known as rotary...
Electron Microscope Tomography and Single-particle Reconstruction01:07

Electron Microscope Tomography and Single-particle Reconstruction

Transmission electron microscopy (TEM) can be used to determine the 3D structure of biological samples with the help of techniques such as electron microscope tomography and single-particle reconstruction. While single-particle reconstruction can examine macromolecules and macromolecular complexes in vitro conditions only, tomography permits the study of cell components or small cells in vivo.
Electron Tomography
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Immunogold Electron Microscopy01:20

Immunogold Electron Microscopy

Immunoelectron microscopy utilizes immunogold labeling of endogenous proteins with specific antibodies to detect and localize these proteins in cells and tissues. The procedure provides insights into the distribution and quantification of protein under different stimulation conditions offering clues about their functions. Conjugating highly electron-dense gold particles with primary or secondary antibodies allow antigen detection on and within cells, with high resolution and specificity.
Overview of Cell-Matrix Interactions01:24

Overview of Cell-Matrix Interactions

The extracellular matrix or ECM holds cells together to form a tissue and allows the cells within the tissue to communicate. ECM comprises proteins such as fibronectin, collagen, laminin, etc. The most abundant protein in this space is collagen. Collagen fibers are interwoven with carbohydrate-containing protein molecules called proteoglycans. ECM allows cell migration and provides a structural scaffold at cell adhesion that anchors the cell when the extracellular matrix proteins interact with...
The Extracellular Matrix01:42

The Extracellular Matrix

In order to maintain tissue organization, many animal cells are surrounded by structural molecules that make up the extracellular matrix (ECM). Together, the molecules in the ECM maintain the structural integrity of tissue as well as the remarkable specific properties of certain tissues.Composition of the Extracellular MatrixThe extracellular matrix (ECM) is commonly composed of ground substance, a gel-like fluid, fibrous components, and many structurally and functionally diverse molecules.

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Scanning Electron Microscopy of Macerated Tissue to Visualize the Extracellular Matrix
10:21

Scanning Electron Microscopy of Macerated Tissue to Visualize the Extracellular Matrix

Published on: June 14, 2016

Electron microscopy in cell-matrix research.

Tobias Starborg1, Yinhui Lu, Roger S Meadows

  • 1Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Michael Smith Building, Oxford Road, Manchester, UK.

Methods (San Diego, Calif.)
|April 30, 2008
PubMed
Summary
This summary is machine-generated.

Collagen fibrils form the extracellular matrix (ECM) essential for tissue development. This article details electron microscopy methods for studying collagen fibril structure and assembly, crucial for understanding related diseases.

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Last Updated: Jul 5, 2026

Scanning Electron Microscopy of Macerated Tissue to Visualize the Extracellular Matrix
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09:53

Micropatterning Transmission Electron Microscopy Grids to Direct Cell Positioning within Whole-Cell Cryo-Electron Tomography Workflows

Published on: September 13, 2021

Area of Science:

  • Biochemistry
  • Cell Biology
  • Biophysics

Background:

  • Multicellular tissue development depends on extracellular matrix (ECM) synthesis, particularly collagen fibrils.
  • Collagen fibril assembly (fibrillogenesis) is vital but poorly understood due to fibril complexity.
  • Dysregulation of collagen fibril deposition is implicated in diseases like osteogenesis imperfecta, fibrosis, and cardiovascular disease.

Purpose of the Study:

  • To review electron microscopy methods for studying collagen fibril structure.
  • To explain the challenges in collagen fibril research.
  • To highlight the importance of understanding fibrillogenesis for disease insights.

Main Methods:

  • Review of established electron microscopy techniques.
  • Description of methods suitable for non-crystalline, cross-linked, large biological assemblies.
  • Focus on techniques applicable to collagen fibril structure and assembly.

Main Results:

  • Electron microscopy is the primary technique for collagen fibril investigation.
  • Specific electron microscope methods are effective for visualizing fibril architecture.
  • These methods overcome limitations of conventional biochemical and structural analyses.

Conclusions:

  • Understanding collagen fibril structure and assembly is critical for tissue development.
  • Electron microscopy provides essential tools for advancing collagen research.
  • Further study of fibrillogenesis can lead to new therapeutic strategies for collagen-related diseases.