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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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Sample Preparation and Transfer Protocol for In-Vacuum Long-Wavelength Crystallography on Beamline I23 at Diamond Light Source
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High-pressure cryocooling for capillary sample cryoprotection and diffraction phasing at long wavelengths.

Chae Un Kim1, Quan Hao, Sol M Gruner

  • 1Field of Biophysics, Cornell University, Ithaca, NY 14853, USA.

Acta Crystallographica. Section D, Biological Crystallography
|April 25, 2007
PubMed
Summary

High-pressure cryocooling advances X-ray crystallography by enabling excellent diffraction-quality crystals without cryoprotectants. New methods support phasing and high-throughput studies, reducing reliance on selenomethionine incorporation.

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Area of Science:

  • Structural Biology
  • Biophysics
  • Crystallography

Background:

  • Crystal cryocooling minimizes radiation damage in X-ray crystallography.
  • A novel high-pressure cryocooling method yields high-quality crystals without penetrative cryoprotectants.

Purpose of the Study:

  • To present three new developments in high-pressure cryocooling.
  • To enhance capabilities for X-ray crystallography and structural biology.

Main Methods:

  • Xenon-Helium (Xe-He) high-pressure cryocooling for single-wavelength anomalous diffraction (SAD) phasing.
  • Native sulfur SAD phasing.
  • Cryopreservation in thick-walled capillaries using only mother liquor.

Main Results:

  • Successful Xe-He cryocooling for Xe SAD phasing.
  • Enabling native sulfur SAD phasing.
  • Demonstrating cryopreservation without additional cryoprotectants.

Conclusions:

  • These advancements facilitate structural solution of proteins without selenomethionine.
  • The methods are beneficial for high-throughput protein crystallography.
  • High-pressure cryocooling offers a versatile approach for crystal preservation and analysis.