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Related Concept Videos

X-ray Diffraction of Biological Samples01:10

X-ray Diffraction of Biological Samples

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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...
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Cryo-electron Microscopy01:28

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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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X-ray Crystallography02:18

X-ray Crystallography

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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.
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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...
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Viral Structure00:56

Viral Structure

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Viruses are extraordinarily diverse in shape and size, but they all have several structural features in common. All viruses have a core that contains a DNA- or RNA-based genome. The core is surrounded by a protective coat of proteins called the capsid. The capsid is composed of subunits called capsomeres. The capsid and genome-containing core are together known as the nucleocapsid.
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X-Ray Crystallography of Viruses.

Núria Verdaguer1, Cristina Ferrer-Orta2, Damià Garriga3

  • 1Institut de Biologia Molecular de Barcelona (CSIC), Parc Científic de Barcelona, Barcelona, Spain. nvmcri@ibmb.csic.es.

Sub-Cellular Biochemistry
|December 31, 2024
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Summary

X-ray crystallography has long been key for determining virus structures. Advances in detectors and automation, alongside cryo-electron microscopy (cryo-EM), are revolutionizing viral research and drug discovery.

Keywords:
Molecular replacementNon-crystallographic symmetryPhase problemStructural virologyViral proteinsVirus X-ray crystallographyVirus capsid

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Area of Science:

  • Structural Biology
  • Virology
  • Biophysics

Background:

  • X-ray crystallography has been the primary method for high-resolution virus structure determination for decades.
  • Increasing complexity of viral structures has driven advancements in X-ray macromolecular crystallography (MX).

Purpose of the Study:

  • To present the common principles of protein and virus crystallography.
  • To highlight the specific aspects of virus structure studies using X-ray crystallography.

Main Methods:

  • X-ray crystallography (MX) for determining virus structures at near-atomic resolution.
  • Advancements in detector technology and automation at synchrotron and X-ray free-electron laser facilities.
  • Cryo-electron microscopy (cryo-EM) for high-resolution structural analysis of large viral particles.

Main Results:

  • X-ray crystallography has significantly advanced our understanding of the viral world.
  • New MX technologies enable high-throughput screening crucial for antiviral drug design.
  • Cryo-EM now offers comparable resolution to MX, becoming a preferred method for large viral assemblies.

Conclusions:

  • Modern X-ray crystallography techniques and cryo-EM are transforming viral structure determination.
  • These advancements are critical for understanding viruses and developing new antiviral therapies.