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Related Experiment Video

Updated: Jul 12, 2026

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
08:53

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

Published on: October 2, 2017

FIP: a highly automated beamline for multiwavelength anomalous diffraction experiments.

M Roth1, P Carpentier, O Kaïkati

  • 1Laboratoire de Cristallographie et Cristallogenèse des Protèines (LCCP), Institut de Biologie Structurale J.-P. Ebel CEA-CNRS, 41 Rue Jules Horowitz, 38027 Grenoble CEDEX 1, France.

Acta Crystallographica. Section D, Biological Crystallography
|April 27, 2002
PubMed
Summary

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The French Collaborating Research Group (CRG) beamline at the European Synchrotron Radiation Facility (ESRF) offers advanced crystallography for biological macromolecules. Its automated system facilitates challenging structure determination using multiwavelength anomalous diffraction.

Area of Science:

  • Structural Biology
  • Crystallography
  • Biophysics

Background:

  • The European Synchrotron Radiation Facility (ESRF) hosts specialized beamlines for macromolecular crystallography.
  • The French Collaborating Research Group (CRG) beamline (FIP) is dedicated to advancing biological macromolecule crystallography.

Purpose of the Study:

  • To describe the capabilities and performance of the FIP beamline.
  • To highlight its utility for challenging structural biology studies.

Main Methods:

  • Utilizes a cryocooled double-crystal monochromator and grazing-angle mirrors for optimal beam delivery.
  • Employs multiwavelength anomalous diffraction (MAD) data collection in the 0.7-1.81 Å wavelength range.
  • Features high levels of automation, including automated crystal centring and data collection management.

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Fully Autonomous Characterization and Data Collection from Crystals of Biological Macromolecules
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Fully Autonomous Characterization and Data Collection from Crystals of Biological Macromolecules

Published on: March 22, 2019

Sample Preparation and Transfer Protocol for In-Vacuum Long-Wavelength Crystallography on Beamline I23 at Diamond Light Source
10:32

Sample Preparation and Transfer Protocol for In-Vacuum Long-Wavelength Crystallography on Beamline I23 at Diamond Light Source

Published on: April 23, 2021

Related Experiment Videos

Last Updated: Jul 12, 2026

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
08:53

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

Published on: October 2, 2017

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

Sample Preparation and Transfer Protocol for In-Vacuum Long-Wavelength Crystallography on Beamline I23 at Diamond Light Source
10:32

Sample Preparation and Transfer Protocol for In-Vacuum Long-Wavelength Crystallography on Beamline I23 at Diamond Light Source

Published on: April 23, 2021

Main Results:

  • The beamline provides an optimal X-ray beam for crystallography in the specified energy range.
  • Automated features simplify beamline operation and data processing.
  • Numerous challenging macromolecular structures have been solved since its inception in 1999.

Conclusions:

  • The FIP beamline is a powerful and user-friendly resource for biological crystallography.
  • Its advanced optics and automation enable efficient determination of complex molecular structures.
  • FIP significantly contributes to structural biology research at the ESRF.