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Related Concept Videos

Determination of Crystal Structures01:29

Determination of Crystal Structures

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...
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
Electron tomography can be performed either in TEM or STEM (scanning transmission...
X-ray Crystallography02:18

X-ray Crystallography

The size of the unit cell and the arrangement of atoms in a crystal may be determined from measurements of the diffraction of X-rays by the crystal, termed X-ray crystallography.
Diffraction
Diffraction is the change in the direction of travel experienced by an electromagnetic wave when it encounters a physical barrier whose dimensions are comparable to those of the wavelength of the light. X-rays are electromagnetic radiation with wavelengths about as long as the distance between neighboring...
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...
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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Related Experiment Video

Updated: Jul 9, 2026

Structure Solution of the Fluorescent Protein Cerulean Using MeshAndCollect
06:42

Structure Solution of the Fluorescent Protein Cerulean Using MeshAndCollect

Published on: March 19, 2019

Combining X-ray and electron-microscopy data to solve crystal structures.

Jorge Navaza1

  • 1Laboratoire de Microscopie Electronique Structurale, Institut de Biologie Structurale Jean-Pierre Ebel, 41 Rue Jules Horowitz, F-38027 Grenoble, France. jorge.navaza@ibs.fr

Acta Crystallographica. Section D, Biological Crystallography
|December 21, 2007
PubMed
Summary

Low-resolution electron microscopy models serve as valuable search tools for molecular replacement. This technique aids in constructing complex multimeric protein models from viral and oligomeric protein data.

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Microcrystal Electron Diffraction of Small Molecules
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Microcrystal Electron Diffraction of Small Molecules

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Last Updated: Jul 9, 2026

Structure Solution of the Fluorescent Protein Cerulean Using MeshAndCollect
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Published on: March 19, 2019

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
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Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

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Microcrystal Electron Diffraction of Small Molecules
09:48

Microcrystal Electron Diffraction of Small Molecules

Published on: March 15, 2021

Area of Science:

  • Structural Biology
  • Biophysics
  • Biochemistry

Background:

  • Molecular replacement (MR) is a key technique for solving protein structures.
  • High-resolution structural data is often required for successful MR.
  • Low-resolution electron microscopy (EM) reconstructions offer an alternative data source.

Purpose of the Study:

  • To demonstrate the utility of low-resolution EM reconstructions as search models in MR.
  • To present a method for generating multimeric models for MR using EM data.
  • To validate the approach across different biological systems.

Main Methods:

  • Utilizing low-resolution EM maps as search models for molecular replacement.
  • Combining EM reconstructions with existing monomeric structures.
  • Generating and refining multimeric models for structural analysis.

Main Results:

  • Successful application of low-resolution EM reconstructions in molecular replacement.
  • Generation of accurate multimeric models for viral, subviral, and oligomeric proteins.
  • Demonstrated feasibility and effectiveness of the described technique.

Conclusions:

  • Low-resolution EM data is a viable resource for molecular replacement.
  • The described method facilitates the structural determination of complex protein assemblies.
  • This approach expands the toolkit for structural biologists.