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Related Experiment Videos

The 'fingerprint' that X-rays can leave on structures.

R B Ravelli1, S M McSweeney

  • 1EMBL Grenoble outstation, Grenoble, BP 156, 38042, France. ravelli@embl-grenoble.fr.

Structure (London, England : 1993)
|April 4, 2000
PubMed
Summary

X-ray crystallography can cause radiation damage to biomacromolecules, altering protein structures and potentially affecting results. Researchers observed changes like increased B factors and broken disulphide bonds, even at low doses.

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Area of Science:

  • Structural biology
  • Biophysics
  • Radiation chemistry

Background:

  • Ionizing radiation damages biomacromolecules via free radicals.
  • X-ray crystallography, a key technique for structure determination, uses ionizing X-rays.
  • Understanding radiation damage is crucial to avoid bias in crystallographic structures.

Purpose of the Study:

  • To investigate the impact of X-ray radiation damage on protein structures determined by crystallography.
  • To identify specific structural changes induced by radiation at doses relevant to experimental conditions.

Main Methods:

  • Investigated radiation damage effects on three different proteins using X-ray crystallography.
  • Analyzed changes in atomic B factors, unit-cell volumes, molecular positions, and chemical modifications.

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Main Results:

  • Observed increased atomic B factors and unit-cell volumes across all tested proteins.
  • Documented molecular rotations, translations, breakage of disulphide bonds, and decarboxylation of acidic residues.
  • These effects lead to significant non-isomorphism, even at doses achievable during routine data collection.

Conclusions:

  • X-ray radiation leaves a detectable 'fingerprint' on protein structures, even at cryogenic temperatures.
  • Radiation-induced non-isomorphism can impede crucial phasing methods like MIR and MAD.
  • Structural changes, such as disulphide bond cleavage and decarboxylation, can precede traditional indicators of radiation damage.