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X-ray Crystallography02:18

X-ray Crystallography

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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...
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X-ray Diffraction of Biological Samples01:10

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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...
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Crystal Field Theory - Octahedral Complexes02:58

Crystal Field Theory - Octahedral Complexes

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Crystal Field Theory
To explain the observed behavior of transition metal complexes (such as colors), a model involving electrostatic interactions between the electrons from the ligands and the electrons in the unhybridized d orbitals of the central metal atom has been developed. This electrostatic model is crystal field theory (CFT). It helps to understand, interpret, and predict the colors, magnetic behavior, and some structures of coordination compounds of transition metals.
CFT focuses on...
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Crystal Field Theory - Tetrahedral and Square Planar Complexes02:46

Crystal Field Theory - Tetrahedral and Square Planar Complexes

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Tetrahedral Complexes
Crystal field theory (CFT) is applicable to molecules in geometries other than octahedral. In octahedral complexes, the lobes of the dx2−y2 and dz2 orbitals point directly at the ligands. For tetrahedral complexes, the d orbitals remain in place, but with only four ligands located between the axes. None of the orbitals points directly at the tetrahedral ligands. However, the dx2−y2 and dz2 orbitals (along the Cartesian axes) overlap with the ligands less than the dxy,...
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Interference and Diffraction02:18

Interference and Diffraction

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Interference is a characteristic phenomenon exhibited by waves. When two electromagnetic waves interact with their peaks and troughs coinciding, a resulting wave with enhanced amplitude is produced. This is known as constructive interference. In this case, the two waves interacting are in phase with each other.
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Mass Spectrometry: Complex Analysis01:21

Mass Spectrometry: Complex Analysis

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Mass spectrometry is an important technique for the identification of pure compounds. However, it has some limitations for the analysis of complex mixtures, often due to excessive fragmentation making the spectrum too complicated to decipher. Mass spectrometry can be combined with suitable separation methods in sequence, forming hyphenated methods, which are useful in the analysis of complex mixtures.
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Related Experiment Video

Updated: Feb 15, 2026

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
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Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

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The Pex4p-Pex22p complex from Hansenula polymorpha: biophysical analysis, crystallization and X-ray diffraction

Ameena M Ali1, Jack Atmaj1, Alaa Adawy1

  • 1Groningen Research Institute of Pharmacy, University of Groningen, 9700 AD Groningen, The Netherlands.

Acta Crystallographica. Section F, Structural Biology Communications
|February 6, 2018
PubMed
Summary

The Pex4p-Pex22p complex is crucial for peroxisome biogenesis, facilitating the recycling of the Pex5p receptor. Its structure reveals insights into how this complex ensures proper protein import into peroxisomes.

Keywords:
Hansenula polymorphaPex22Pex4peroxisome importubiquitin-conjugating enzyme

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

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Peroxisomes are vital eukaryotic organelles involved in diverse metabolic functions.
  • Peroxisome biogenesis depends on PEX genes encoding peroxin proteins.
  • Matrix proteins are imported post-translationally, with PTS1-containing proteins relying on the Pex5p receptor.

Purpose of the Study:

  • To elucidate the structural basis of the Pex4p-Pex22p complex's function in peroxisome biogenesis.
  • To understand the role of the Pex4p-Pex22p complex in Pex5p receptor recycling and PTS1 protein import.

Main Methods:

  • Crystallization of Pex4p and the Pex4p-Pex22p complex from Hansenula polymorpha.
  • X-ray diffraction data collection to high resolution (2.0 and 2.85 Å).

Main Results:

  • The crystal structures of Pex4p and the Pex4p-Pex22p complex were determined.
  • These structures provide a molecular basis for the Pex4p-Pex22p complex's function.

Conclusions:

  • The Pex4p-Pex22p complex is essential for monoubiquitination of Pex5p, a key step in its recycling.
  • Understanding the Pex4p-Pex22p structure will illuminate the mechanism of peroxisome biogenesis and PTS1 import.