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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...
Infrared (IR) Spectroscopy: Overview01:09

Infrared (IR) Spectroscopy: Overview

When electromagnetic radiation passes through a material, atoms or molecules transition from a lower to a higher energy state by absorbing radiation corresponding to the energy difference between the two states. The absorption of infrared (IR) radiation causes transitions between vibrational energy levels in a molecule. Therefore, IR spectroscopy is a useful analytical tool for determining the molecular structure of molecules.
Different compounds display unique properties due to their...
IR Spectrometers01:25

IR Spectrometers

There are two main infrared (IR) spectrophotometers: dispersive IR spectrometers and Fourier transform infrared (FTIR) spectrometers. In a dispersive IR spectrometer, a beam of infrared radiation produced by a hot wire is divided into two parallel equal-intensity beams using mirrors. One beam passes through the sample, while another is a reference beam. The beams then move through the monochromator, which separates the radiations into a continuous spectrum of different frequencies. The...
Total Internal Reflection Fluorescence Microscopy01:05

Total Internal Reflection Fluorescence Microscopy

Total internal reflection fluorescence microscopy or TIRF is an advanced microscopic technique used to visualize fluorophores in samples close to a solid surface with a higher refractive index, such as a glass coverslip. TIRF only allows fluorophores in proximity to the solid surface to be excited. When light from a medium with a lower refractive index (such as air) hits the glass coverslip at a critical angle, the light undergoes total internal reflection stead of passing through the glass.
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...

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Related Experiment Video

Updated: Jun 3, 2026

On-Chip Crystallization and Large-Scale Serial Diffraction at Room Temperature
07:42

On-Chip Crystallization and Large-Scale Serial Diffraction at Room Temperature

Published on: March 11, 2022

Infrared protein crystallography.

J Timothy Sage1, Yunbin Zhang, John McGeehan

  • 1Department of Physics and Center for Interdisciplinary Research on Complex Systems, Northeastern University, Boston, MA 02115, USA. jtsage@neu.edu

Biochimica Et Biophysica Acta
|March 8, 2011
PubMed
Summary
This summary is machine-generated.

Infrared spectroscopy on oriented protein crystals reveals molecular details. Polarized measurements enhance structural analysis, complementing X-ray crystallography by identifying specific molecular orientations and interactions.

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

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Protein Crystallization for X-ray Crystallography
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Protein Crystallization for X-ray Crystallography

Published on: January 16, 2011

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Last Updated: Jun 3, 2026

On-Chip Crystallization and Large-Scale Serial Diffraction at Room Temperature
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On-Chip Crystallization and Large-Scale Serial Diffraction at Room Temperature

Published on: March 11, 2022

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

Published on: June 27, 2014

Protein Crystallization for X-ray Crystallography
09:27

Protein Crystallization for X-ray Crystallography

Published on: January 16, 2011

Area of Science:

  • Biophysics
  • Structural Biology
  • Spectroscopy

Background:

  • Infrared spectroscopy is a powerful tool for studying protein structure and function.
  • Understanding protein behavior in crystalline states is crucial for structural biology.
  • Exploiting molecular orientation in protein crystals can provide unique insights.

Purpose of the Study:

  • To explore the application of infrared spectroscopy to protein crystals, focusing on polarization measurements.
  • To investigate how molecular orientation in single crystals can be exploited.
  • To compare infrared spectra of proteins in crystals versus solutions.

Main Methods:

  • Utilizing infrared microscopes for transmission measurements on individual protein crystals.
  • Employing flow cells for ligand-induced spectral changes and cryostreams for flash-cooled crystals.
  • Performing polarized infrared measurements (dichroism) on oriented single crystals.

Main Results:

  • Infrared spectroscopy can probe conformational distributions in crystals and solutions, often showing similar equilibria but perturbed kinetics.
  • Polarized infrared measurements reveal molecular orientation, distinguish spectral contributions from similar sites, and identify hydrogen bonding partners.
  • X-ray-induced products like CO(2) can be detected, and infrared dichroism synergizes with X-ray crystallography for crystals with favorable symmetry.

Conclusions:

  • Polarized infrared spectroscopy on oriented protein crystals offers unique advantages for structural and functional analysis.
  • This technique complements X-ray crystallography by providing complementary information on molecular orientation and interactions.
  • Infrared spectroscopy is valuable for understanding protein behavior in the crystalline state and its relation to solution conditions.