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Updated: Jun 13, 2026

Optimizing the Growth of Endothiapepsin Crystals for Serial Crystallography Experiments
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Hyperquenching for protein cryocrystallography.

Matthew Warkentin1, Viatcheslav Berejnov, Naji S Husseini

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

Journal of Applied Crystallography
|September 28, 2011
PubMed
Summary
This summary is machine-generated.

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Removing the cold gas layer during plunge cooling significantly enhances cryo-cooling rates for protein crystals. This advancement reduces the need for cryoprotectants, simplifying sample preparation for X-ray crystallography.

Area of Science:

  • Crystallography
  • Biophysics
  • Materials Science

Background:

  • Plunge cooling of protein crystals in liquid cryogens typically involves significant heat transfer in the gas layer above the liquid.
  • Current methods often rely on cryoprotectants to prevent ice crystal formation, which can complicate crystallization screening and analysis.

Purpose of the Study:

  • To investigate the impact of removing the cold gas layer during plunge cooling on sample cooling rates.
  • To determine the effect of this modified cooling technique on the cryoprotectant requirements for protein crystals.

Main Methods:

  • Experimental setup designed to eliminate the cold gas layer during plunge cooling of samples in liquid nitrogen or propane.
  • Measurement of cooling rates for various sample sizes and plunge velocities.

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Last Updated: Jun 13, 2026

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  • Assessment of glycerol concentrations required to prevent ice crystallization in aqueous solutions.

    • Main Results:

    • Cooling rates increased to 1.5 × 10(4) K s(-1) for small samples, a 100-fold improvement over existing methods.
    • Required glycerol concentrations decreased from ~28% w/v to as low as 6% w/v.
    • The findings explain previously observed discrepancies in diffraction quality between plunge cooling and gas-stream cooling.

    Conclusions:

    • Eliminating the cold gas layer during plunge cooling dramatically enhances cooling efficiency for protein crystallography samples.
    • Reduced or eliminated need for cryoprotectants simplifies sample preparation and may improve crystallization screening.
    • This technique offers a pathway to obtain better diffraction data by optimizing the sample cooling process.