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X-ray Diffraction of Biological Samples01:10

X-ray Diffraction of Biological Samples

X-ray diffraction or XRD is an analytical tool that utilizes X-rays to study ordered structures such as crystalline organic and inorganic samples, polycrystalline materials, proteins, carbohydrates, and drugs.
According to Bragg's law, when X-rays strike the sample positioned on a stage, the rays are  scattered by the electron clouds around the sample atoms. The  X-ray diffraction or scattering is caused by constructive interference of the X-ray waves that reflect off the internal crystal...
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In the late 1800s, the revelation that light extended beyond visible wavelengths led to the discovery of X-rays by Wilhelm Roentgen. Recognized as high-energy electromagnetic radiation with short wavelengths, X-rays prompted exploration into their interaction with crystals. Max von Laue proposed in 1912 that the periodic arrangement of atoms, ions, or molecules in crystals would cause them to diffract X-rays, a hypothesis confirmed through experiments with copper sulfate and zinc sulfide...
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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...
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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.
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Microcrystal Electron Diffraction of Small Molecules
09:48

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Published on: March 15, 2021

Electron diffraction and high-resolution imaging on highly-crystalline β-chitin microfibril.

Yu Ogawa1, Satoshi Kimura, Masahisa Wada

  • 1Department of Biomaterials Science, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Yayoi 1-1-1, Bunkyo-ku, Tokyo 113-8657, Japan.

Journal of Structural Biology
|July 21, 2011
PubMed
Summary

This study reveals the ultrastructure of beta-chitin microfibrils in diatoms and tubeworms using advanced microscopy. Findings support existing models and propose a new molecular packing model for beta-chitin.

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Area of Science:

  • Biomaterials Science
  • Structural Biology
  • Marine Biology

Background:

  • Beta-chitin is a crucial biopolymer found in various organisms.
  • Understanding its ultrastructure is key to unlocking its material properties.

Purpose of the Study:

  • To investigate the ultrastructure of beta-chitin microfibrils from Thalassiosira (diatom) and Lamellibrachia (tubeworm).
  • To validate existing structural models of beta-chitin crystals.
  • To propose a molecular packing model for beta-chitin microfibrils.

Main Methods:

  • High-resolution electron microscopy (HREM) on ultrathin sections.
  • Electron diffraction techniques, including electron microdiffraction.
  • Analysis of cross-sectional shapes and lattice fringes.

Main Results:

  • Electron diffraction data supported the anhydrous beta-chitin crystal structure model.
  • HREM revealed distinct microfibril cross-sectional shapes: rectangular for Thalassiosira and parallelogram for Lamellibrachia.
  • Clear observation of (010) plane lattice fringes in both microfibril types.

Conclusions:

  • The study confirms the structural model of anhydrous beta-chitin crystals.
  • A novel molecular packing model for beta-chitin microfibrils has been constructed based on experimental data.
  • This research provides insights into the structural organization of beta-chitin in different biological systems.