Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Determination of Crystal Structures01:29

Determination of Crystal Structures

In the late 1800s, the revelation that light extended beyond visible wavelengths led to the discovery of X-rays by Wilhelm Roentgen. Recognized as high-energy electromagnetic radiation with short wavelengths, X-rays prompted exploration into their interaction with crystals. Max von Laue proposed in 1912 that the periodic arrangement of atoms, ions, or molecules in crystals would cause them to diffract X-rays, a hypothesis confirmed through experiments with copper sulfate and zinc sulfide...
Crystal Growth: Principles of Crystallization01:25

Crystal Growth: Principles of Crystallization

Crystallization is a phase transformation process in which crystals are precipitated from a supersaturated solution or formed from other sources. During crystallization, atoms or molecules arrange themselves into a well-defined, rigid crystal lattice to minimize energy.
Initiating crystallization involves manipulating the concentration of the solute and the temperature of the solution. Since crystal growth occurs when the ratio of concentration and solubility of the solute in the solvent – the...
Recrystallization: Solid–Solution Equilibria01:10

Recrystallization: Solid–Solution Equilibria

Recrystallization is a purification technique used to separate impurities from solid compounds. In this technique, no chemical reactions occur. Instead, it exploits physical properties only, specifically, the solubility differences between the desired compound and impurities, either at a single temperature or at different temperatures, and under other selected conditions. The solid-solution equilibrium (solubility equilibrium) of each component in the solution represents a binary phase...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Towards light-coupled sample preparation for time-resolved cryoEM studies.

IUCrJ·2026
Same author

Drop-on-fixed-target reaction initiation approach for serial and time-resolved crystallography.

IUCrJ·2026
Same author

Generation and modulation of catalytically relevant states of a dye-decolourizing peroxidase using time-resolved serial femtosecond crystallography with drop-on-chip mixing and X-ray-driven reduction.

Acta crystallographica. Section D, Structural biology·2026
Same author

Experience with the Jungfrau-1M detector at Diamond Light Source.

Journal of synchrotron radiation·2026
Same author

Integrated structural dynamics uncover a new B<sub>12</sub> photoreceptor activation mode.

Nature·2026
Same author

Increasing X-ray energy improves data quality in serial crystallography.

Journal of synchrotron radiation·2026

Related Experiment Video

Updated: Jul 18, 2026

Optimization of Crystal Growth for Neutron Macromolecular Crystallography
12:29

Optimization of Crystal Growth for Neutron Macromolecular Crystallography

Published on: March 13, 2021

Cryocrystallography of macromolecules: practice and optimization.

Elspeth Garman1, Robin L Owen

  • 1Department of Biochemistry, Laboratory of Molecular Biophysics, University of Oxford, Oxford, UK.

Methods in Molecular Biology (Clifton, N.J.)
|December 19, 2006
PubMed
Summary

Flash-cooling protein crystals using cryocrystallography significantly reduces radiation damage, enabling complete datasets from single crystals. This guide provides step-by-step protocols for optimizing cryo-procedures for better structural data.

More Related Videos

Optimizing the Growth of Endothiapepsin Crystals for Serial Crystallography Experiments
09:52

Optimizing the Growth of Endothiapepsin Crystals for Serial Crystallography Experiments

Published on: February 4, 2021

An All-in-one Sample Holder for Macromolecular X-ray Crystallography with Minimal Background Scattering
07:55

An All-in-one Sample Holder for Macromolecular X-ray Crystallography with Minimal Background Scattering

Published on: July 6, 2019

Related Experiment Videos

Last Updated: Jul 18, 2026

Optimization of Crystal Growth for Neutron Macromolecular Crystallography
12:29

Optimization of Crystal Growth for Neutron Macromolecular Crystallography

Published on: March 13, 2021

Optimizing the Growth of Endothiapepsin Crystals for Serial Crystallography Experiments
09:52

Optimizing the Growth of Endothiapepsin Crystals for Serial Crystallography Experiments

Published on: February 4, 2021

An All-in-one Sample Holder for Macromolecular X-ray Crystallography with Minimal Background Scattering
07:55

An All-in-one Sample Holder for Macromolecular X-ray Crystallography with Minimal Background Scattering

Published on: July 6, 2019

Area of Science:

  • Structural Biology
  • Biophysics

Background:

  • Cryocrystallography is a standard technique for protein crystal data collection.
  • Flash-cooling to cryogenic temperatures (around 100K) minimizes X-ray radiation damage.
  • This preservation extends crystal lifetime for complete dataset acquisition.

Purpose of the Study:

  • To provide detailed, step-by-step guidelines for flash-cooling protein crystals.
  • To explain the rationale behind recommended cryo-cooling procedures.
  • To highlight the impact of cryo-protocol optimization on data quality and structure solution.

Main Methods:

  • Detailed protocols for flash-cooling protein crystals to cryogenic temperatures.
  • Explanation of the underlying principles of reduced radiation damage at low temperatures.
  • Guidance on optimizing the entire cryo-protocol for improved experimental outcomes.

Main Results:

  • Flash-cooling dramatically reduces radiation damage compared to room temperature data collection.
  • Optimized cryo-protocols lead to substantial improvements in data resolution and quality.
  • Attention to procedural details positively impacts the final dataset's utility for structure determination.

Conclusions:

  • Standardized and optimized flash-cooling techniques are crucial for successful cryocrystallography.
  • Implementing detailed cryo-protocols enhances the efficiency and success rate of protein structure determination.
  • Best practices in cryo-cooling are essential for obtaining high-quality structural data.