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Neutron and X‐ray single‐crystal diffraction from protein microcrystals via magnetically oriented microcrystal arrays in gels
Author(s) -
Tsukui Shu,
Kimura Fumiko,
Kusaka Katsuhiro,
Baba Seiki,
Mizuno Nobuhiro,
Kimura Tsunehisa
Publication year - 2016
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.374
H-Index - 138
ISSN - 2059-7983
DOI - 10.1107/s2059798316007415
Subject(s) - neutron diffraction , diffraction , materials science , protein crystallization , crystallography , resolution (logic) , lysozyme , x ray crystallography , neutron , self healing hydrogels , single crystal , neutron reflectometry , crystal structure , chemistry , optics , neutron scattering , crystallization , small angle neutron scattering , physics , polymer chemistry , organic chemistry , biochemistry , quantum mechanics , artificial intelligence , computer science
Protein microcrystals magnetically aligned in D 2 O hydrogels were subjected to neutron diffraction measurements, and reflections were observed for the first time to a resolution of 3.4 Å from lysozyme microcrystals (∼10 × 10 × 50 µm). This result demonstrated the possibility that magnetically oriented microcrystals consolidated in D 2 O gels may provide a promising means to obtain single‐crystal neutron diffraction from proteins that do not crystallize at the sizes required for neutron diffraction structure determination. In addition, lysozyme microcrystals aligned in H 2 O hydrogels allowed structure determination at a resolution of 1.76 Å at room temperature by X‐ray diffraction. The use of gels has advantages since the microcrystals are measured under hydrated conditions.