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Updated: Jul 3, 2026
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The Automated Crystallography Pipelines at the EMBL HTX Facility in Grenoble
Published on: June 5, 2021
High-throughput crystallization-to-structure pipeline at RIKEN SPring-8 Center.
Michihiro Sugahara1, Yukuhiko Asada, Katsumi Shimizu
1Advanced Protein Crystallography Research Group, RIKEN SPring-8 Center, Harima Institute, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo, 679-5148, Japan.
Journal of Structural and Functional Genomics
|August 5, 2008
Summary
A new automated pipeline for X-ray crystallography was developed to determine protein structures efficiently. This high-throughput system successfully determined 138 crystal structures, advancing structural genomics.
Area of Science:
- Structural biology
- Biophysics
- Crystallography
Background:
- Structural genomics requires efficient methods for determining protein structures.
- Automating X-ray crystallography can accelerate structure determination.
Purpose of the Study:
- To describe a newly developed high-throughput crystallization-to-structure pipeline for structural genomics.
- To detail the automated technologies integrated into the pipeline.
Main Methods:
- Development and implementation of the automated crystallization and observation robot system (TERA).
- Utilization of the SPring-8 Precise Automatic Cryosample Exchanger (SPACE) for automated data collection.
- Application of the Package of Expert Researcher's Operation Network (PERON) for automated crystallographic computation.
Main Results:
- The pipeline was used by seven researchers over five years (starting April 2002).
- 138 independent crystal structures were determined.
- The process involved 437 purified proteins, 234 cryoloop-mountable crystals, and 175 diffraction data sets.
Conclusions:
- The described high-throughput pipeline significantly enhances the efficiency of protein structure determination.
- The integrated automated systems (TERA, SPACE, PERON) facilitate rapid structural genomics research.
