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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 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...
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...

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Sample Preparation and Transfer Protocol for In-Vacuum Long-Wavelength Crystallography on Beamline I23 at Diamond Light Source
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A dipicolinate lanthanide complex for solving protein structures using anomalous diffraction.

Guillaume Pompidor1, Olivier Maury, Jean Vicat

  • 1Institut de Biologie Structurale J.-P. Ebel, UMR 5075, 41 Rue Jules Horowitz, Grenoble, France.

Acta Crystallographica. Section D, Biological Crystallography
|July 8, 2010
PubMed
Summary
This summary is machine-generated.

Lanthanide tris-dipicolinate complexes facilitate protein crystallography by forming derivative crystals. This method enables high-quality electron-density maps for structural determination, advancing protein science.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Crystallography

Background:

  • Protein crystallography is crucial for understanding biological function.
  • Phase determination is a key challenge in protein crystallography.
  • Lanthanide complexes offer potential as heavy atom derivatives.

Purpose of the Study:

  • To evaluate lanthanide tris-dipicolinate complexes as derivatization agents for protein crystallography.
  • To determine the binding mode and utility of these complexes across various proteins.
  • To assess the impact on diffraction quality and electron-density map resolution.

Main Methods:

  • Preparation of derivative crystals using six different proteins and lanthanide tris-dipicolinate complexes.
  • Collection of X-ray diffraction data using synchrotron and laboratory sources.
  • Structure determination and refinement utilizing anomalous scattering of lanthanides.

Main Results:

  • Successful preparation of derivative crystals for all six tested proteins.
  • High-quality electron-density maps were obtained, enabling accurate phase determination.
  • Characterization of the binding mode, involving interactions between ligand carboxylates and protein hydrogen-bond donors.
  • Identification of enantiomeric selection based on binding site topology.
  • Discovery of a new monoclinic C2 crystal form for hen egg-white lysozyme and xylanase.

Conclusions:

  • Lanthanide tris-dipicolinate complexes are effective agents for protein derivatization in crystallography.
  • The method provides a reliable route to high-resolution protein structures.
  • Enantiomeric specificity in binding offers insights into protein-ligand interactions.