Frontiers in Protein Crystallography Using Quantum Beams

Dear Colleagues,

X-ray protein crystallography has been a leader in life sciences. However, until now, most of the structural analysis of membrane proteins, which has greatly contributed to structure-based drug design, has been performed by cryo-electron microscopy. It has gradually become clear that the results of structural analysis using X-ray protein crystallography (especially when including metals, such as Fe, Cu, and Zn) are having an effect due to the radiation of X-ray, which hits the constituent atoms of the protein and knocks out electrons, exposing the protein material to a reducing atmosphere.

Then, what will be the new frontiers in protein crystallography? The X-ray free-electron laser is attracting attention as a new frontier, as it provides all the X-ray diffraction data, including time-resolved diffraction data, before the effect of X-ray radiation. There is also no such concern with neutron protein crystallography, and moreover this provides information on hydrogen, hydration, and protonation states, which are essential for understanding the mechanisms of physiological functions. The use of meson as a new quantum beam can be considered. The holography of metalloprotein crystals is such that the valence states of the active metal at the active center of the metalloprotein can be determined, and this will be very promising in the future. It is, therefore, a good chance to explore these new frontiers, which may surpass conventional X-ray protein crystallography, in our Special Issue entitled “Frontiers in Protein Crystallography Using Quantum Beams”.

Prof. Dr. Nobuo Niimura
Prof. Dr. So Iwata
Guest Editors

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• X-ray free-electron laser
• no radiation effect
• neutron protein crystallography
• hydrogen
• hydration
• protonation
• holography
• meson