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Beamline for Biological Macromolecular Assemblies at SPring-8 (BL44XU)
Operating since March 1999
2001 Installed Image Plate – CCD hybrid detector (DIP6040)
2002 Installed N2-cooled double crystal monochromator
2005, 2006 Installed new goniomator
2006 Upgrade control system
2010 Beam stabilization and introduction of coaxial microscope
2011 Installed high-speed goniomator
2012 Installed high-speed large area CCD detector (MX300HE)
2013 Beam stabilization
2014 Installed vertical mirror

The beamline for X-ray crystallography of biological macromolecules at SPring-8 is operated by the Institute for Protein Research. This beamline is available to researchers who belong to academic organizations throughout the world. Regular applications involving non-proprietary proposals are received once per year, and urgent applications can be accepted all year around. About 40 to 50% of the total beamtime is used for collaborative research programs of the Institute for Protein Research. This beamline is specially designed for data collection on analyzing biological macromolecular assembly crystals, such as protein complexes, protein-nucleic acid complexes, and viruses.

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Analytical Apparatus for Supra-biomolecules
Operating since March 1999

Knowledge of the chemical structures of biomolecules is indispensable for understanding their biological functions and roles. However, since they are typically obtained in limited amounts and consisting of various molecules with diverse chemical properties, their structures are difficult to analyze with conventional methods. The analytical apparatus for supra-biomolecules is a tandem mass spectrometer (MS/MS) equipped with the electrospray ionization method. It allows the detection of biomolecules at sub-picomole levels, especially proteins, peptides, and sugar chains of glycoproteins, and is used for their structural analyses.

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Solid-state NMR Spectrometers
All the spectrometers were installed in March 2002 and replaced with new ones in March, 2014

The spectrometers are used for analyzing the structures, dynamics, and functions of biomolecules in non-crystalline solid states, such as proteins in lipid bilayers and amyloid proteins. High-resolution NMR experiments are performed at 。¹H resonance frequencies of 500, 600, and 700 MHz. The two spectrometers are equipped with frequency-tunable gyrotrons generating terahertz waves and sample-rotation systems at cryogenic temperatures. Thereby, they provide the world’s highest performance in NMR systems.

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Solution NMR Spectrometer in an Ultra-high Magnetic Field
Operating since August 2010, following installation in March 2010

The NMR spectrometer with an 。¹H resonance frequency of 950 MHz enables the analysis of 3D structures and interactions of high molecular-weight proteins and organic molecules at low concentrations, which markedly exceeds the performance of conventional spectrometers. This device provides one of the world’s highest magnetic fields, following a 1000 MHz spectrometer in France.

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High-performance X-ray Diffractometer
Operating since August 2003
2011.2 Upgraded to high-brilliance

This system has two high-performance image plate detectors (Rigaku R-AXIS IV and R-AXIS VII) combined with a high-intensity rotating-anode X-ray generator (Rigaku FR-E) and confocal mirrors (Rigaku VariMax HF and CMF-MicroMax). This system gives a top-level performance X-ray diffraction data collection system for protein crystallography.