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Slow cooling and temperature-controlled protein crystallography.

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  • 1Physics Department, Cornell University, Ithaca, NY 14853, USA.

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Slowly cooling protein crystals to 100 K without cryoprotectants is possible by removing external solvent. This slow cooling method offers an alternative to flash cooling for diffraction studies across a wide temperature range.

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Area of Science:

  • Structural Biology
  • Biophysics
  • Crystallography

Background:

  • Rapid cooling is standard in cryocrystallography to prevent ice crystal formation and sample damage.
  • Cryoprotectants are typically used to mitigate these issues during cooling.

Purpose of the Study:

  • To investigate an alternative cooling method for protein crystals.
  • To determine if slow cooling is feasible without penetrating cryoprotectants.

Main Methods:

  • Careful and complete removal of external solvent from protein crystals.
  • Slow cooling of protein crystals to 100 K at a rate of 0.1 K/s.

Main Results:

  • Protein crystals were successfully cooled to 100 K using slow cooling without cryoprotectants.
  • This method is viable when flash cooling is not effective.

Conclusions:

  • Removing external solvent enables slow cooling of protein crystals.
  • This technique provides a valuable alternative for cryocrystallography, allowing diffraction studies from 300 K down to 100 K.