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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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Fully Autonomous Characterization and Data Collection from Crystals of Biological Macromolecules
07:11

Fully Autonomous Characterization and Data Collection from Crystals of Biological Macromolecules

Published on: March 22, 2019

Racemic protein crystallography.

Todd O Yeates1, Stephen B H Kent

  • 1Department of Chemistry and Biochemistry, University of California, Los Angeles, California 90095, USA. yeates@mbi.ucla.edu

Annual Review of Biophysics
|March 27, 2012
PubMed
Summary
This summary is machine-generated.

Chemically synthesized mirror-image proteins, or racemic protein mixtures, can crystallize more easily than natural proteins. This breakthrough offers new avenues for protein crystallography and structure determination.

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Protein Crystallization for X-ray Crystallography

Published on: January 16, 2011

Area of Science:

  • Biochemistry
  • Structural Biology
  • Crystallography

Background:

  • Proteins are naturally chiral, existing in a single 'handedness'.
  • Chemical synthesis enables the creation of mirror-image protein forms (enantiomers).
  • Racemic mixtures combine both enantiomeric forms of a protein.

Purpose of the Study:

  • To review recent advancements in racemic protein crystallography.
  • To explore the potential of racemic protein mixtures in crystallization and structure determination.
  • To highlight the impact of improved synthetic methods on protein crystallography.

Main Methods:

  • Review of theoretical predictions and experimental data on racemic protein crystallization.
  • Discussion of crystallization strategies for racemic protein mixtures.
  • Examination of advances in chemical synthesis for protein production.

Main Results:

  • Racemic protein mixtures show high amenability to crystallization, exceeding natural protein capabilities.
  • Crystals from racemic mixtures provide unique advantages for structure determination.
  • Synthetic methods are increasingly capable of producing larger proteins for crystallography.

Conclusions:

  • Racemic protein crystallography presents a promising new frontier in structural biology.
  • The ability to crystallize enantiomeric protein mixtures expands possibilities in protein structure analysis.
  • Continued advances in synthesis and crystallization techniques will further unlock the potential of racemic protein crystallography.