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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...
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...
Scanning Electron Microscopy01:07

Scanning Electron Microscopy

A scanning electron microscope (SEM) is used to study the surface features of a sample by using an electron beam that scans the sample surface in a two-dimensional manner. Typically, areas between ~1 centimeter to 5 micrometers in width can be imaged. SEM can be used to image bacteria, viruses, tissues as well as larger samples like insects. Conventional SEM gives a magnification ranging from 20X to 30,000X and spatial resolution of 50 to 100 nanometers.
Fundamental Principles
Accelerated...
Electron Microscope Tomography and Single-particle Reconstruction01:07

Electron Microscope Tomography and Single-particle Reconstruction

Transmission electron microscopy (TEM) can be used to determine the 3D structure of biological samples with the help of techniques such as electron microscope tomography and single-particle reconstruction. While single-particle reconstruction can examine macromolecules and macromolecular complexes in vitro conditions only, tomography permits the study of cell components or small cells in vivo.
Electron Tomography
Electron tomography can be performed either in TEM or STEM (scanning transmission...
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...
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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Synchrotron X-ray Microdiffraction and Fluorescence Imaging of Mineral and Rock Samples
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Using electron microscopy to complement X-ray powder diffraction data to solve complex crystal structures.

Lynne B McCusker1, Christian Baerlocher

  • 1Laboratory of Crystallography, ETH Zurich, CH-8093, Zurich, Switzerland. mccusker@mat.ethz.ch

Chemical Communications (Cambridge, England)
|March 12, 2009
PubMed
Summary

Combining high-resolution X-ray powder diffraction and electron microscopy data enables crystal structure determination for complex polycrystalline materials. This integrated approach overcomes limitations of conventional methods, revealing intricate structures like novel zeolites.

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Area of Science:

  • Crystallography
  • Materials Science
  • Electron Microscopy

Background:

  • Crystal structure determination is crucial for understanding material properties.
  • Conventional methods face challenges with complex polycrystalline materials.
  • Electron microscopy and X-ray diffraction offer complementary data.

Purpose of the Study:

  • To demonstrate the synergistic use of high-resolution X-ray powder diffraction and electron microscopy for crystal structure determination.
  • To tackle complex polycrystalline materials resistant to conventional analysis.
  • To improve structure solution accuracy by integrating diverse data types.

Main Methods:

  • Utilizing high-resolution transmission electron microscopy (HRTEM) for crystallographic phase information.
  • Employing precession electron diffraction (PED) for identifying weak reflections and improving intensity partitioning.
  • Applying dual-space structure determination programs (Focus and pCF) to combine diffraction and real-space data.

Main Results:

  • Successfully determined the complex crystal structures of three novel zeolites: TNU-9, IM-5, and SSZ-74.
  • Demonstrated that integrating HRTEM and PED data enhances the solution of challenging structures.
  • Showcased the effectiveness of Focus and pCF programs in handling combined crystallographic datasets.

Conclusions:

  • The combined approach of X-ray powder diffraction and electron microscopy is powerful for complex crystal structure determination.
  • This integrated strategy significantly advances the analysis of polycrystalline materials.
  • The method provides a robust pathway for solving intricate zeolite frameworks and other advanced materials.