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Related Concept Videos

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...

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A Sample Preparation Pipeline for Microcrystals at the VMXm Beamline
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A Sample Preparation Pipeline for Microcrystals at the VMXm Beamline

Published on: June 17, 2021

In situ macromolecular crystallography using microbeams.

Danny Axford1, Robin L Owen, Jun Aishima

  • 1Life Science Division, Diamond Light Source, Harwell Science and Innovation Campus, Didcot, Oxfordshire OX11 0DE, England.

Acta Crystallographica. Section D, Biological Crystallography
|April 25, 2012
PubMed
Summary
This summary is machine-generated.

In situ data collection in macromolecular crystallography bypasses crystal handling and cryoprotection issues. This method enables structure solution from weakly diffracting samples using microfocus X-ray beams.

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Microcrystallography of Protein Crystals and In Cellulo Diffraction

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Microcrystallography of Protein Crystals and In Cellulo Diffraction
09:35

Microcrystallography of Protein Crystals and In Cellulo Diffraction

Published on: July 21, 2017

Area of Science:

  • Structural Biology
  • Biophysics
  • Crystallography

Background:

  • Macromolecular crystallography is crucial for determining protein structures.
  • Crystal production and handling are significant bottlenecks in the structure determination process.
  • Current methods often require cryoprotection, which can alter crystal properties.

Purpose of the Study:

  • To present an in situ data collection method for macromolecular crystallography.
  • To overcome challenges associated with traditional crystal handling and cryoprotection.
  • To demonstrate the utility of microfocus X-ray beams for in situ analysis.

Main Methods:

  • Utilizing a dedicated goniometer on the I24 microfocus beamline at Diamond Light Source.
  • Recording diffraction data directly from crystals within their crystallization plates at room temperature.
  • Employing an intense and flexible microfocus beam for in situ diffraction analysis.

Main Results:

  • Successfully assessed weakly diffracting samples with good signal-to-noise ratio.
  • Overcame background scatter from crystallization plates.
  • Achieved structure solution for bovine enterovirus 2.
  • Facilitated crystallization screening of membrane proteins and complexes.
  • Enabled structure solution from high-throughput pipeline crystallization hits.

Conclusions:

  • In situ data collection is a viable strategy to streamline macromolecular crystallography.
  • This approach minimizes crystal handling and cryoprotection artifacts.
  • Microbeam technology significantly enhances the potential for in situ structure determination.