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Control of strain in subgrains of protein crystals by the introduction of grown‐in dislocations
Author(s) -
Koizumi Haruhiko,
Uda Satoshi,
Suzuki Ryo,
Tachibana Masaru,
Kojima Kenichi,
Tsukamoto Katsuo,
Yoshizaki Izumi,
Fukuyama Seijiro,
Suzuki Yoshihisa
Publication year - 2021
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/s2059798321001820
Subject(s) - protein crystallization , crystal (programming language) , materials science , strain (injury) , crystallography , diffraction , x ray crystallography , dislocation , stress (linguistics) , condensed matter physics , optics , chemistry , crystallization , physics , biology , computer science , linguistics , philosophy , organic chemistry , anatomy , programming language
It is important to reveal the exact cause of poor diffractivity in protein crystals in order to determine the accurate structure of protein molecules. It is shown that there is a large amount of local strain in subgrains of glucose isomerase crystals even though the overall crystal quality is rather high, as shown by clear equal‐thickness fringes in X‐ray topography. Thus, a large stress is exerted on the subgrains of protein crystals, which could significantly lower the resistance of the crystals to radiation damage. It is also demonstrated that this local strain can be reduced through the introduction of dislocations in the crystal. This suggests that the introduction of dislocations in protein crystals can be effective in enhancing the crystal quality of subgrains of protein crystals. By exploiting this effect, the radiation damage in subgrains could be decreased, leading to the collection of X‐ray diffraction data sets with high diffractivity.