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Related Concept Videos

Cryo-electron Microscopy01:28

Cryo-electron Microscopy

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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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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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Related Experiment Video

Updated: Jul 24, 2025

Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy
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Uncovering Protein Ensembles: Automated Multiconformer Model Building for X-ray Crystallography and Cryo-EM.

Stephanie A Wankowicz1, Ashraya Ravikumar1, Shivani Sharma2,3

  • 1Department of Bioengineering and Therapeutic Sciences, University of California San Francisco, San Francisco, CA, USA.

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qFit software now better models biomolecular conformational heterogeneity. This automated strategy improves protein structural models derived from experimental data, aiding research into macromolecular dynamics and function.

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Area of Science:

  • Structural Biology
  • Computational Biology
  • Biochemistry

Background:

  • Biomolecules exist in multiple conformational states essential for function.
  • Traditional methods like X-ray crystallography and cryo-electron microscopy (cryo-EM) yield ensemble-averaged data.
  • Current modeling often represents only a single conformation, failing to capture biomolecular complexity.

Conclusions:

  • qFit's automated approach reduces the difficulty of creating multiconformer models.
  • Facilitates the development of new hypotheses linking macromolecular dynamics to function.
  • Enables more accurate representation of biomolecular structures based on experimental data.