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Updated: Jun 7, 2026

Neutron Crystallography Data Collection and Processing for Modelling Hydrogen Atoms in Protein Structures
Published on: December 1, 2020
Neutron structure analysis using the IBARAKI biological crystal diffractometer (iBIX) at J-PARC.
Ichiro Tanaka1, Katsuhiro Kusaka, Takaaki Hosoya
1Ibaraki University, Japan. i.tanaka@mx.ibaraki.ac.jp
The new IBARAKI Biological Crystal Diffractometer (iBIX) at J-PARC shows high performance for protein crystallography. This advanced instrument is now collecting its first full protein crystal data set.
Area of Science:
- Neutron scattering
- Protein crystallography
- Materials science
Background:
- The Japan Proton Accelerator Research Complex (J-PARC) is a leading facility for advanced scientific research.
- Neutron diffraction is a powerful technique for determining the structure of materials at the atomic level.
- Protein crystallography is essential for understanding biological functions and developing new drugs.
Purpose of the Study:
- To introduce the IBARAKI Biological Crystal Diffractometer (iBIX) as a new instrument for protein crystallography.
- To report on the initial performance and operational status of iBIX.
- To demonstrate the capability of iBIX for collecting high-quality diffraction data.
Main Methods:
- Construction and commissioning of the iBIX diffractometer at J-PARC.
- Preliminary structure analyses using organic crystals.
- Operation at 120 kW beam power.
- Data collection from a protein crystal.
Main Results:
- The iBIX diffractometer has been successfully constructed and operational since December 2008.
- Preliminary analyses confirmed high performance of iBIX, even at 120 kW operation.
- The first full data set from a protein crystal is currently being collected.
Conclusions:
- iBIX is a high-performance diffractometer for protein crystallography.
- The instrument is ready for advanced structural studies at J-PARC.
- iBIX will contribute to significant advancements in structural biology.
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