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Related Concept Videos

Preparation of Samples for Electron Microscopy01:20

Preparation of Samples for Electron Microscopy

To be visualized by an electron microscope, either transmission or scanning, biological samples need to be fixed (stabilized) so the electron beam does not destroy them and dried thoroughly (desiccated/dehydrated) so the vacuum does not affect them. Fixation needs to be done as quickly as possible because the sample properties will start changing as soon as it is removed from its natural environment. For example, in a tissue sample, the oxygen levels begin decreasing, causing an altered...
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...
Fixation and Sectioning01:03

Fixation and Sectioning

Two basic types of preparation are used to visualize specimens with a light microscope: wet mounts and fixed specimens.
The simplest type of preparation is the wet mount, in which the specimen is placed in a drop of liquid on the slide. A liquid specimen can be directly deposited on the slide using a dropper. Solid specimens, such as skin scraping, can be placed on the slide before adding a drop of liquid to prepare the wet mount. Sometimes the liquid is simply water, but stains are often added...
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...

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A Sample Preparation Pipeline for Microcrystals at the VMXm Beamline
09:00

A Sample Preparation Pipeline for Microcrystals at the VMXm Beamline

Published on: June 17, 2021

Specimen preparation for electron diffraction of thin crystals.

Huaibin Wang1, Kenneth H Downing

  • 1Life Sciences Division, Lawrence Berkeley National Laboratory, Donner Laboratory, 1 Cyclotron Road, Berkeley, CA 94720, United States.

Micron (Oxford, England : 1993)
|June 22, 2010
PubMed
Summary

Electron crystallography enables high-resolution structural analysis of 2-D protein crystals. This study focuses on specimen preparation techniques to improve crystal flatness for better electron diffraction data collection.

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Area of Science:

  • Structural Biology
  • Biophysics
  • Materials Science

Background:

  • Electron crystallography is a key technique for determining the structure of 2-D protein crystals.
  • High-resolution structural information from radiation-sensitive samples relies on averaging methods.
  • Cryo-electron crystallography, using image and diffraction data, has solved numerous protein structures.

Purpose of the Study:

  • To discuss specimen preparation methods for electron crystallographic data collection of 2-D protein crystals.
  • To emphasize factors influencing crystal flatness for improved data quality.
  • To cover specific data collection protocols for 2-D protein crystals.

Main Methods:

  • Specimen preparation techniques for preserving native state and order in hydrated samples.
  • Methods to address challenges in electron diffraction data collection, especially at high tilt angles.
  • Protocols for collecting electron diffraction data from 2-D protein crystals.

Main Results:

  • Development of methods for preserving samples in a near-native, hydrated state.
  • Identification of factors affecting crystal flatness, crucial for reducing diffraction spot blurring.
  • Discussion of specialized data collection strategies for 2-D protein crystals.

Conclusions:

  • Effective specimen preparation is vital for high-resolution electron crystallography of 2-D protein crystals.
  • Improving crystal flatness is essential for obtaining clear electron diffraction data.
  • Optimized data collection protocols enhance structural characterization using electron crystallography.