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Updated: Aug 9, 2026

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The Automated Crystallography Pipelines at the EMBL HTX Facility in Grenoble
Published on: June 5, 2021
The ID23-1 structural biology beamline at the ESRF
Didier Nurizzo1, Trevor Mairs, Matias Guijarro
1European Synchrotron Radiation Facility, BP-220, F-38043 Grenoble CEDEX 09, France. nurizzo@esrf.fr
Journal of Synchrotron Radiation
|April 29, 2006
Summary
The European Synchrotron Radiation Facility (ESRF) developed a new automated beamline, ID23-1, to meet rising demand for macromolecular crystallography synchrotron time. This innovative system enhances protein crystallography research efficiency.
Area of Science:
- Structural Biology
- Biophysics
- Materials Science
Background:
- Increasing demand for synchrotron beamtime impacts macromolecular crystallography (MC).
- The European Synchrotron Radiation Facility (ESRF) addresses this by constructing a novel dual-station beamline.
- This initiative aims to enhance MC research capabilities and accessibility.
Purpose of the Study:
- To introduce ID23-1, the first station of a new dual-station beamline at ESRF.
- To detail the technical specifications and automation features of the ID23-1 beamline.
- To highlight the development of a user-friendly software suite and diagnostic tools.
Main Methods:
- Construction of a dual station beamline utilizing a canted undulator X-ray source.
- Implementation of a tunable, MAD-capable station (ID23-1) with a mini-focus X-ray beam.
- Integration of a channel-cut monochromator and toroidal mirror for X-ray beam focusing.
Main Results:
- ID23-1 is operational, offering a tunable, MAD-capable station with a mini-focus X-ray beam.
- A new software suite enhances user and staff operation, enabling an industrial-like environment.
- Integrated diagnostics facilitate rapid troubleshooting and beamline maintenance.
Conclusions:
- The ID23-1 beamline successfully increases synchrotron access for macromolecular crystallography.
- The developed automation and software are transferable to other ESRF beamlines and synchrotrons.
- This advancement supports efficient and accessible protein crystallography research.

