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Studying the Cytoskeleton01:17

Studying the Cytoskeleton

The cytoskeletal architecture can be studied using different microscopic and biochemical techniques. Electron microscopy was instrumental in discovering the cytoskeletal architecture around the 1960s, which allowed obtaining structural information at a high-resolution level. However, the sample preparation procedure often limits this ability in biological samples. Several protocols have been developed over the years to optimize sample preparation. In one of the protocols known as rotary...

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Related Experiment Video

Updated: May 15, 2026

Purification of Human S100A12 and Its Ion-induced Oligomers for Immune Cell Stimulation
12:55

Purification of Human S100A12 and Its Ion-induced Oligomers for Immune Cell Stimulation

Published on: September 29, 2019

X-ray structural analysis of S100 proteins.

Günter Fritz1

  • 1Department of Neuropathology, Neurozentrum, University of Freiburg, Freiburg, Germany. guenter.fritz@uniklinik-freiburg.de

Methods in Molecular Biology (Clifton, N.J.)
|January 9, 2013
PubMed
Summary

X-ray crystallography provides rapid, detailed structural insights into S100 proteins. This method allows for the analysis of S100 proteins in various states, revealing crucial information about their function.

Area of Science:

  • Structural biology
  • Biochemistry

Background:

  • S100 proteins are a family of calcium-binding proteins involved in various cellular processes.
  • Understanding their structure is crucial for elucidating their function and interactions.

Purpose of the Study:

  • To present a general method for isolating and crystallizing S100 proteins.
  • To detail the structural analysis of S100 protein crystals using synchrotron X-ray diffraction.

Main Methods:

  • Protein isolation and purification techniques.
  • X-ray crystallography for crystal growth.
  • High-resolution data collection at a synchrotron source.
  • Analysis of crystallographic data to determine protein structure.

Main Results:

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Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
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Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

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Related Experiment Videos

Last Updated: May 15, 2026

Purification of Human S100A12 and Its Ion-induced Oligomers for Immune Cell Stimulation
12:55

Purification of Human S100A12 and Its Ion-induced Oligomers for Immune Cell Stimulation

Published on: September 29, 2019

Expression, Purification, and Antimicrobial Activity of S100A12
11:10

Expression, Purification, and Antimicrobial Activity of S100A12

Published on: May 13, 2017

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
09:15

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

Published on: January 10, 2018

  • Successful crystallization of S100 proteins in apo and metal ion-bound states (Ca(2+), Zn(2+)).
  • High-resolution diffraction data obtained, enabling detailed structural determination.
  • Identification of ion-binding sites, protein conformation, and potential target interaction surfaces.

Conclusions:

  • X-ray crystallography is an effective and efficient technique for S100 protein structure determination.
  • The described methods facilitate the structural study of S100 proteins in different functional states.
  • Structural insights gained are vital for understanding S100 protein mechanisms and interactions.