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High resolution cryogenic transmission electron microscopy study of Escherichia coli Dps protein: First direct observation in quasinative stateстатья
Статья опубликована в высокорейтинговом журнале
Статья опубликована в журнале из списка Web of Science и/или Scopus- Авторы: Antipov S.S., Pichkur E.B., Praslova N.V., Preobrazhenskaya E.V., Usoltseva D.S., Belikov E.A., Chuvenkova O.A., Presnyakov M.Yu, Artyukhov V.G., Ozoline O.N., Turishchev S.Yu
- Журнал: Results in Physics
- Том: 11
- Год издания: 2018
- Первая страница: 926
- Последняя страница: 928
- DOI: 10.1016/j.rinp.2018.10.059
- Аннотация: The Dps protein of Escherichia coli is a homododecamer with an internal cavity accumulating iron oxides, transformed from ambient toxic Fe2+ into a harmless inorganic core. High resolution cryogenic transmission electron microscopy was applied to visualize the protein molecules and to characterize their ability to self-organization. Due to ultrafast freezing, the Dps dodecameric particles were observed as a “snapshot” of their natural state, and highly ordered two-dimensional layers with hexagonal symmetry were obtained. Thus, it became clear, that “super structured monolayers”, spanning over several thousand square nanometers can be formed under certain cryogenic regimes.
- Добавил в систему: Озолинь Ольга Николаевна