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Related Concept Videos

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...
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...
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...
Protein Diffusion in the Membrane01:24

Protein Diffusion in the Membrane

Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...

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Updated: Jun 5, 2026

Native Cell Membrane Nanoparticles System for Membrane Protein-Protein Interaction Analysis
07:31

Native Cell Membrane Nanoparticles System for Membrane Protein-Protein Interaction Analysis

Published on: July 16, 2020

X-ray diffraction from membrane protein nanocrystals.

M S Hunter1, D P DePonte, D A Shapiro

  • 1Department of Chemistry and Biochemistry, Arizona State University, Tempe, Arizona, USA.

Biophysical Journal
|December 31, 2010
PubMed
Summary
This summary is machine-generated.

Serial nanocrystallography enables membrane protein structure determination from small crystals. This method overcomes X-ray damage, paving the way for molecular-resolution maps of vital membrane proteins.

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Microcrystallography of Protein Crystals and In Cellulo Diffraction

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Area of Science:

  • Structural Biology
  • Biophysics
  • Biochemistry

Background:

  • Membrane proteins are crucial cellular components, yet their structural determination is challenging.
  • Fewer than 300 unique membrane protein structures are known, hindering research.
  • Existing methods face limitations, particularly X-ray damage to small crystals.

Purpose of the Study:

  • To explore serial nanocrystallography for membrane protein structure determination.
  • To assess the suitability of small membrane protein crystals for structural analysis.
  • To overcome limitations in current membrane protein structure determination techniques.

Main Methods:

  • Serial nanocrystallography using a liquid jet delivery system at room temperature.
  • Collection of X-ray powder diffraction data from Photosystem I nanocrystals (100 nm to 2 μm).
  • Analysis of data from crystals containing fewer than 100 unit cells.

Main Results:

  • Demonstrated suitability of membrane protein crystals with < 100 unit cells for structural investigation.
  • Showcased serial nanocrystallography's ability to mitigate X-ray damage in small crystals.
  • Collected diffraction data from integral membrane protein Photosystem I.

Conclusions:

  • Serial nanocrystallography is a viable method for determining membrane protein structures.
  • Future integration with X-ray free-electron lasers could yield high-resolution maps.
  • This technique expands possibilities for studying essential membrane proteins.