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Related Concept Videos

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...
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...
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...

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Related Experiment Video

Updated: Jun 5, 2026

An All-in-one Sample Holder for Macromolecular X-ray Crystallography with Minimal Background Scattering
07:55

An All-in-one Sample Holder for Macromolecular X-ray Crystallography with Minimal Background Scattering

Published on: July 6, 2019

Developments in low-resolution biological X-ray crystallography.

Fred Dyda1

  • 1Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK), National Institutes of Health Bethesda, MD 20892 USA.

F1000 Biology Reports
|December 21, 2010
PubMed
Summary
This summary is machine-generated.

Solving macromolecular structures with X-ray crystallography remains difficult at low resolutions (worse than 3.5Å). This report reviews recent advances that help overcome these challenges in crystallographic studies.

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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

Related Experiment Videos

Last Updated: Jun 5, 2026

An All-in-one Sample Holder for Macromolecular X-ray Crystallography with Minimal Background Scattering
07:55

An All-in-one Sample Holder for Macromolecular X-ray Crystallography with Minimal Background Scattering

Published on: July 6, 2019

Microcrystallography of Protein Crystals and In Cellulo Diffraction
09:35

Microcrystallography of Protein Crystals and In Cellulo Diffraction

Published on: July 21, 2017

Microfluidic Chips for In Situ Crystal X-ray Diffraction and In Situ Dynamic Light Scattering for Serial Crystallography
11:48

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
  • Crystallography

Background:

  • X-ray crystallography is crucial for determining molecular structures.
  • Low-resolution diffraction (<3.5Å) poses significant challenges for structure determination.
  • Large molecules and complex assemblies often yield low-resolution data.

Purpose of the Study:

  • To summarize recent technological and methodological advancements in X-ray crystallography.
  • To address the persistent challenges in solving and refining low-resolution structures.
  • To provide an overview of new strategies for low-resolution crystallographic work.

Main Methods:

  • Review of recent literature and technological developments in X-ray crystallography.
  • Analysis of strategies specifically designed for low-resolution data.
  • Focus on techniques applicable to large molecules and multicomponent assemblies.

Main Results:

  • Several new approaches and technologies have emerged to aid low-resolution crystallography.
  • These advances improve the ability to solve and refine structures from limited diffraction data.
  • Progress has been made in handling data from challenging crystalline samples.

Conclusions:

  • Recent advances offer promising solutions for low-resolution X-ray crystallography.
  • These developments are vital for studying large and complex biological assemblies.
  • Continued innovation is expected to further improve structural determination at lower resolutions.