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Related Concept Videos

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: Jul 6, 2026

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
10:03

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

Published on: June 27, 2014

Hemoprotein time-resolved X-ray crystallography.

Mario Milani1, Marco Nardini, Alessandra Pesce

  • 1Department of Biomolecular Sciences and Biotechnology, University of Milano, I-20131 Milano, Italy. mario.milani@mi.infm.it

IUBMB Life
|April 2, 2008
PubMed
Summary
This summary is machine-generated.

Structural dynamics control protein function, studied via time-resolved crystallography. Researchers examined myoglobin dynamics, revealing ligand diffusion events in hemoproteins using flash photolysis and X-ray diffraction.

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The Automated Crystallography Pipelines at the EMBL HTX Facility in Grenoble
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The Automated Crystallography Pipelines at the EMBL HTX Facility in Grenoble
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The Automated Crystallography Pipelines at the EMBL HTX Facility in Grenoble

Published on: June 5, 2021

Area of Science:

  • Biophysics
  • Structural Biology
  • Protein Dynamics

Background:

  • Investigating the role of structural dynamics in protein function is crucial for understanding biological processes.
  • Advanced experimental techniques are increasingly employed to study dynamic aspects of protein structure-function relationships.
  • Time-resolved crystallography offers experimental evidence for protein dynamics, despite practical challenges.

Purpose of the Study:

  • To provide an overview of dynamical properties in myoglobin and related hemoproteins.
  • To highlight dynamical events associated with diatomic ligand diffusion to and from the heme group.
  • To showcase the utility of time-resolved methods for studying transient intermediates in hemoproteins.

Main Methods:

  • Utilized time-resolved crystallography combined with flash photolysis techniques.
  • Employed Laue X-ray diffraction to capture rapid structural changes.
  • Studied photosensitive heme-Fe--ligand bonds in model hemoproteins.

Main Results:

  • Experimental evidence was obtained on the dynamical properties of myoglobin and homologous hemoproteins.
  • Transient intermediates were successfully studied, providing insights into protein dynamics.
  • Key dynamical events characterizing diatomic ligand diffusion to/from the heme were highlighted.

Conclusions:

  • Time-resolved crystallography is a valuable tool for elucidating protein dynamics and structure-function relationships.
  • The study provides insights into the dynamic behavior of hemoproteins, specifically concerning ligand interactions.
  • Understanding these dynamics is essential for comprehending the functional mechanisms of these proteins.