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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...
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...
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...
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...

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Updated: Jun 8, 2026

On-Chip Crystallization and Large-Scale Serial Diffraction at Room Temperature
07:42

On-Chip Crystallization and Large-Scale Serial Diffraction at Room Temperature

Published on: March 11, 2022

3D reconstruction from 2D crystal image and diffraction data.

Andreas D Schenk1, Daniel Castaño-Díez, Bryant Gipson

  • 1Department of Cell Biology, Harvard Medical School, Boston, Massachusetts, USA.

Methods in Enzymology
|October 5, 2010
PubMed
Summary
This summary is machine-generated.

Electron crystallography determines high-resolution structures of membrane proteins using 2D protein crystals. This study details image-processing algorithms and software (2dx, XDP, IPLT) for analyzing electron microscopy data.

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Last Updated: Jun 8, 2026

On-Chip Crystallization and Large-Scale Serial Diffraction at Room Temperature
07:42

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Published on: March 11, 2022

Microcrystallography of Protein Crystals and In Cellulo Diffraction
09:35

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Published on: July 21, 2017

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Microfluidic Chips for In Situ Crystal X-ray Diffraction and In Situ Dynamic Light Scattering for Serial Crystallography

Published on: April 24, 2018

Area of Science:

  • Structural biology
  • Biophysics
  • Biochemistry

Background:

  • High-resolution structure determination of membrane proteins is crucial for understanding their function.
  • Electron crystallography of 2D protein crystals offers a powerful approach for this purpose.

Purpose of the Study:

  • To introduce image-processing algorithms for electron crystallography of 2D protein crystals.
  • To demonstrate the application of Medical Research Council (MRC) programs and specific software packages (2dx, XDP, IPLT).

Main Methods:

  • Utilizing electron microscopy to record images or diffraction patterns from frozen hydrated 2D protein crystals.
  • Applying crystallographic Fourier space-based image-processing algorithms.
  • Employing software packages including 2dx, XDP, and IPLT for data analysis.

Main Results:

  • Successful implementation of image-processing algorithms for electron crystallography.
  • Demonstrated utility of MRC programs and associated software for 3D protein structure determination.
  • High-resolution structural data can be obtained from membrane-embedded proteins.

Conclusions:

  • Electron crystallography provides a high-resolution method for determining membrane protein structures.
  • The presented image-processing algorithms and software facilitate the analysis of electron microscopy data.
  • This approach aids in advancing the understanding of membrane protein function through structural biology.