Abstract
The IBARAKI biological crystal diffractometer, iBIX, is a high-performance time-of-flight neutron single-crystal diffractometer for elucidating mainly the hydrogen, protonation and hydration structures of biological macromolecules in various life processes. Since the end of 2008, iBIX has been available to users' experiments supported by Ibaraki University. Since August 2012, an upgrade of the 14 existing detectors has begun and 16 new detectors have been installed for iBIX. The total measurement efficiency of the present diffractometer has been improved by one order of magnitude from the previous one with the increasing of accelerator power. In December 2012, commissioning of the new detectors was successful, and collection of the diffraction dataset of ribonucrease A as a standard protein was attempted in order to estimate the performance of the upgraded iBIX in comparison with previous results. The resolution of diffraction data, equivalence among intensities of symmetry-related reflections and reliability of the refined structure have been improved dramatically. iBIX is expected to be one of the highest-performance neutron single-crystal diffractometers for biological macromolecules in the world.
Highlights
Hydrogen atoms and water molecules around proteins play a very important role in the stability of the three-dimensional structure and in many physiological functions of them
The development of a neutron imaging plate (NIP) and a diffractometer equipped with a NIP on reactor neutron sources has been a breakthrough event in neutron protein crystallography and has met the demand on structural biology in the life science field (Niimura & Bau, 2008)
Since August 2012, the new detector system has been adapted such that the 14 existing detectors have been upgraded and 16 new detectors have been installed for iBIX
Summary
Hydrogen atoms and water molecules around proteins play a very important role in the stability of the three-dimensional structure and in many physiological functions of them. The demand on positional information of hydrogen atoms in a protein molecule has been increasing after many projects in the world in which thousands of protein structures have been analyzed. The development of a neutron imaging plate (NIP) and a diffractometer equipped with a NIP on reactor neutron sources has been a breakthrough event in neutron protein crystallography and has met the demand on structural biology in the life science field (Niimura & Bau, 2008). The demand on neutron structural biology in the current life science field has increased continuously, neutron protein crystallography (NPC) still remains to this day a severely limited technique. 994 doi:10.1107/S0909049513021845 neutron structural biology, Ibaraki Prefectural Government in Japan has started to construct a new high-performance time-of-flight (TOF) neutron single-crystal diffractometer (IBARAKI Biological Crystal Diffractometer, iBIX) at the 1 MW pulsed neutron source in J-PARC, for industrial use since 2004. In this paper the current status of iBIX, and the upgraded diffractometer in particular, will be presented
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