Editing Neutron diffraction (section)

=== Current trends in structural biology ===
Modern advancements in neutron diffraction are enhancing data precision, broadening structural research applications, and refining experimental methodologies. A key focus is the improved visualization of hydrogen atoms in biological [[Macromolecule|macromolecules]], crucial for studying [[enzymatic activity]] and [[hydrogen bonding]]. The expansion of specialized [[Diffractometer|diffractometers]] has increased accessibility in structural biology, with techniques like [[Monochrome|monochromatic]], quasi-Laue, and time-of-flight methods being optimized for efficiency. Innovations in sample preparation, particularly protein deuteration, are minimizing [[background noise]] and reducing the need for large crystals. Additionally, [[Computational tools for artificial intelligence|computational tools]], including quantum chemical modeling, are aiding in the interpretation of complex molecular interactions. Improved neutron sources, such as spallation facilities, along with advanced detectors, are further boosting measurement accuracy and structural resolution. These developments are solidifying neutron diffraction as a critical technique for exploring the molecular architecture of biological systems.<ref>{{Cite journal |last1=Kono |first1=Fumiaki |last2=Kurihara |first2=Kazuo |last3=Tamada |first3=Taro |date=2022 |title=Current status of neutron crystallography in structural biology |url=https://www.jstage.jst.go.jp/article/biophysico/19/0/19_e190009/_article |journal=Biophysics and Physicobiology |language=en |volume=19 |pages=e190009 |doi=10.2142/biophysico.bppb-v19.0009 |issn=2189-4779 |pmc=9135615 |pmid=35666700}}</ref>