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      New frontiers in atom probe tomography: a review of research enabled by cryo and/or vacuum transfer systems

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          Abstract

          There has been a recent surge in the use of cryo and/or vacuum specimen preparation and transfer systems to broaden the scope of research enabled by the microscopy technique of atom probe tomography. This is driven by the fact that, as for many microscopes, the application of atom probes to air- and temperature-sensitive materials or wet biological specimens has previously been limited by transfer through air at room temperature. Here we provide an overview of areas of research that benefit from these new transfer and analysis protocols, as well as a review of current advances in transfer devices, environmental cells, and glove boxes for controlled specimen manipulation. This includes the study of catalysis and corrosion, biological samples, liquid-solid interfaces, natural aging, and the distribution of hydrogen in materials.

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          Atomic structure of sensitive battery materials and interfaces revealed by cryo–electron microscopy

          Whereas standard transmission electron microscopy studies are unable to preserve the native state of chemically reactive and beam-sensitive battery materials after operation, such materials remain pristine at cryogenic conditions. It is then possible to atomically resolve individual lithium metal atoms and their interface with the solid electrolyte interphase (SEI). We observe that dendrites in carbonate-based electrolytes grow along the (preferred), , or directions as faceted, single-crystalline nanowires. These growth directions can change at kinks with no observable crystallographic defect. Furthermore, we reveal distinct SEI nanostructures formed in different electrolytes.
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            Self-assembled monolayers of thiolates on metals as a form of nanotechnology.

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              Crystal structure of a neutralizing human IGG against HIV-1: a template for vaccine design.

              We present the crystal structure at 2.7 angstrom resolution of the human antibody IgG1 b12. Antibody b12 recognizes the CD4-binding site of human immunodeficiency virus-1 (HIV-1) gp120 and is one of only two known antibodies against gp120 capable of broad and potent neutralization of primary HIV-1 isolates. A key feature of the antibody-combining site is the protruding, finger-like long CDR H3 that can penetrate the recessed CD4-binding site of gp120. A docking model of b12 and gp120 reveals severe structural constraints that explain the extraordinary challenge in eliciting effective neutralizing antibodies similar to b12. The structure, together with mutagenesis studies, provides a rationale for the extensive cross-reactivity of b12 and a valuable framework for the design of HIV-1 vaccines capable of eliciting b12-like activity.
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                Author and article information

                Journal
                101771735
                49987
                Mater Today Adv
                Mater Today Adv
                Materials today. Advances
                2590-0498
                25 September 2020
                10 July 2020
                September 2020
                22 October 2020
                : 7
                : 100090
                Affiliations
                [a ]Australian Centre for Microscopy and Microanalysis, University of Sydney, Madsen Building F09, NSW 2006, Australia
                [b ]Department of Materials, University of Oxford, Parks Road, Oxford, OX1 3PH, United Kingdom
                [c ]Physical and Computational Sciences Directorate, Pacific Northwest National Laboratory, P.O. Box 999, Richland, WA 99352, USA
                [d ]Environmental Molecular Science Laboratory, Pacific Northwest National Laboratory, P.O. Box 999 Richland, WA 99352, USA
                [e ]School of Aerospace, Mechanical and Mechatronic Engineering, University of Sydney, NSW 2006, Australia
                Author notes
                [* ]Corresponding author. julie.cairney@ 123456sydney.edu.au (J.M. Cairney).
                Article
                NIHMS1626598
                10.1016/j.mtadv.2020.100090
                7581275
                33103106
                c0667df3-2e7d-44b2-91e2-53005ee4f713

                This is an open access article under the CC BY license ( http://creativecommons.org/licenses/by/4.0/).

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                Categories
                Article

                focused ion beam,catalysis,hydrogen,deuterium,organic,cryogenic,ultrahigh vacuum,soft matter

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