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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...
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...
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...

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Related Experiment Video

Updated: Jun 14, 2026

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

Temperature-dependent macromolecular X-ray crystallography.

Martin Weik1, Jacques Philippe Colletier

  • 1CEA, IBS, Laboratoire de Biophysique Moléculaire, F-38054 Grenoble, France. martin.weik@ibs.fr

Acta Crystallographica. Section D, Biological Crystallography
|April 13, 2010
PubMed
Summary
This summary is machine-generated.

This review explores how temperature control in X-ray crystallography, from 15 K to room temperature, reveals macromolecular dynamics and intermediate states. It highlights using X-ray-induced damage for studying these states.

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

Microfluidic Chips for In Situ Crystal X-ray Diffraction and In Situ Dynamic Light Scattering for Serial Crystallography
11:48

Microfluidic Chips for In Situ Crystal X-ray Diffraction and In Situ Dynamic Light Scattering for Serial Crystallography

Published on: April 24, 2018

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Last Updated: Jun 14, 2026

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

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

Microfluidic Chips for In Situ Crystal X-ray Diffraction and In Situ Dynamic Light Scattering for Serial Crystallography
11:48

Microfluidic Chips for In Situ Crystal X-ray Diffraction and In Situ Dynamic Light Scattering for Serial Crystallography

Published on: April 24, 2018

Area of Science:

  • Structural Biology
  • Biophysics
  • Crystallography

Background:

  • X-ray crystallography is crucial for determining biological macromolecule structures.
  • Standard data collection near 100 K minimizes radiation damage.
  • Broader temperature ranges offer insights into macromolecular dynamics and structure.

Purpose of the Study:

  • To review the dynamical behavior of crystalline macromolecules and solvent across cryo-temperatures.
  • To discuss experimental strategies in kinetic crystallography for trapping intermediate states.
  • To explore the utility of X-ray-induced changes in reaction initiation.

Main Methods:

  • Temperature-controlled X-ray crystallography experiments (15 K to room temperature).
  • Kinetic crystallography techniques combining reaction initiation with specific temperature profiles.
  • Utilizing X-ray-induced phenomena for triggering reactions.

Main Results:

  • Cryo-temperature studies reveal dynamical behavior of macromolecules and surrounding solvent.
  • Kinetic crystallography enables the generation and trapping of macromolecular intermediate states.
  • X-ray-induced changes can be harnessed to initiate reactions, offering insights into radiation damage.

Conclusions:

  • Temperature-controlled X-ray crystallography provides valuable dynamical and structural information.
  • Kinetic crystallography is a powerful tool for studying transient states in macromolecules.
  • Understanding and utilizing radiation damage can be beneficial for biochemical studies.