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Related Concept Videos

X-ray Diffraction of Biological Samples01:10

X-ray Diffraction of Biological Samples

X-ray diffraction or XRD is an analytical tool that utilizes X-rays to study ordered structures such as crystalline organic and inorganic samples, polycrystalline materials, proteins, carbohydrates, and drugs.
According to Bragg's law, when X-rays strike the sample positioned on a stage, the rays are  scattered by the electron clouds around the sample atoms. The  X-ray diffraction or scattering is caused by constructive interference of the X-ray waves that reflect off the internal crystal...
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...
X-ray Crystallography02:18

X-ray Crystallography

The size of the unit cell and the arrangement of atoms in a crystal may be determined from measurements of the diffraction of X-rays by the crystal, termed X-ray crystallography.
Diffraction
Diffraction is the change in the direction of travel experienced by an electromagnetic wave when it encounters a physical barrier whose dimensions are comparable to those of the wavelength of the light. X-rays are electromagnetic radiation with wavelengths about as long as the distance between neighboring...
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...

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Related Experiment Video

Updated: Jun 4, 2026

Protein Crystallization for X-ray Crystallography
09:27

Protein Crystallization for X-ray Crystallography

Published on: January 16, 2011

Protein crystallization for X-ray crystallography.

Moshe A Dessau1, Yorgo Modis

  • 1Molecular Biochemistry and Biophysics, Yale University, USA.

Journal of Visualized Experiments : Jove
|February 10, 2011
PubMed
Summary
This summary is machine-generated.

Obtaining high-resolution macromolecular structures via X-ray crystallography requires purified samples. This study details vapor diffusion and batch crystallization methods essential for protein structure determination.

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Automated Protocols for Macromolecular Crystallization at the MRC Laboratory of Molecular Biology
11:20

Automated Protocols for Macromolecular Crystallization at the MRC Laboratory of Molecular Biology

Published on: January 24, 2018

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Last Updated: Jun 4, 2026

Protein Crystallization for X-ray Crystallography
09:27

Protein Crystallization for X-ray Crystallography

Published on: January 16, 2011

Crystallization and In Situ Room Temperature Data Collection Using the Crystallization Facility at Harwell and Beamline VMXi, Diamond Light Source
07:08

Crystallization and In Situ Room Temperature Data Collection Using the Crystallization Facility at Harwell and Beamline VMXi, Diamond Light Source

Published on: March 8, 2024

Automated Protocols for Macromolecular Crystallization at the MRC Laboratory of Molecular Biology
11:20

Automated Protocols for Macromolecular Crystallization at the MRC Laboratory of Molecular Biology

Published on: January 24, 2018

Area of Science:

  • Structural Biology
  • Biochemistry
  • X-ray Crystallography

Background:

  • Determining three-dimensional structures of biological macromolecules is crucial for understanding cellular functions.
  • Atomic resolution structures provide deep insights into protein function and cellular mechanisms.
  • X-ray crystallography, responsible for 86% of Protein Data Bank entries, relies on high-quality crystals.

Purpose of the Study:

  • To explain the importance of macromolecular homogeneity for high-resolution crystallographic studies.
  • To describe the principles of protein crystallization, focusing on achieving supersaturation.
  • To demonstrate experimental setups for vapor diffusion (hanging drop, sitting drop) and batch crystallization.

Main Methods:

  • Macromolecular purification to homogeneity is critical for crystal formation.
  • Concentrating samples to 2-50 mg/mL without aggregation or precipitation is necessary.
  • Techniques include vapor diffusion (hanging drop, sitting drop) and batch crystallization under oil.

Main Results:

  • Vapor diffusion involves controlled dehydration to reach the crystal nucleation zone.
  • Batch crystallization directly mixes protein with precipitant under oil to prevent evaporation.
  • Both methods aim to induce nucleation and growth of three-dimensional crystals.

Conclusions:

  • Macromolecular homogeneity and controlled supersaturation are key to successful crystallization.
  • Vapor diffusion and batch crystallization are established techniques for obtaining protein crystals.
  • These methods facilitate the determination of atomic resolution structures for biological macromolecules.