Atom Probe Tomographic Mapping Directly Reveals the Atomic Distribution of Phosphorus in Resin Embedded Ferritin

Perea, Daniel E.; Liu, Jia; Bartrand, Jonah; Dicken, Quinten; Thevuthasan, S.; Browning, Nigel D.; Evans, James E.

doi:10.1038/srep22321

Cited by 60 publications

(54 citation statements)

References 36 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Preparation of the goethite microrods into needle-shaped tips is challenging but necessary for APT analysis. Currently, there are few successful approaches for the preparation of APT specimens from unsupported nanostructured materials that result in meaningful APT results (28)(29)(30)(31)(32). The goethite microrods in our study were prepared for APT analysis using an encapsulation, cross-sectioning approach (33).…”

Section: Resultsmentioning

confidence: 99%

“…In principle, using isotopic tracers, the APT approach developed here could be adapted to unraveling the mass transfer pathways at the evolving interfaces in this system. Although challenging, APT analysis of the distribution of potassium on amorphous ferrihydrite particles was previously achieved (31). In particular, nanoparticles must be embedded in a matrix without nanovoids or microvoids, which can cause premature fracture or artifacts in APT reconstructions, that preserves their structure and composition to acquire meaningful data that can be related to the original particles (32,51,52).…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Visualizing the iron atom exchange front in the Fe(II)-catalyzed recrystallization of goethite by atom probe tomography

Taylor

Liu

Zhang

et al. 2019

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

View full text Add to dashboard Cite

The autocatalytic redox interaction between aqueous Fe(II) and Fe(III)-(oxyhydr)oxide minerals such as goethite and hematite leads to rapid recrystallization marked, in principle, by an atom exchange (AE) front, according to bulk iron isotopic tracer studies. However, direct evidence for this AE front has been elusive given the analytical challenges of mass-resolved imaging at the nanoscale on individual crystallites. We report successful isolation and characterization of the AE front in goethite microrods by 3D atom probe tomography (APT). The microrods were reacted with Fe(II) enriched in tracer 57Fe at conditions consistent with prior bulk studies. APT analyses and 3D reconstructions on cross-sections of the microrods reveal an AE front that is spatially heterogeneous, at times penetrating several nanometers into the lattice, in a manner consistent with defect-accelerated exchange. Evidence for exchange along microstructural domain boundaries was also found, suggesting another important link between exchange extent and initial defect content. The findings provide an unprecedented view into the spatial and temporal characteristics of Fe(II)-catalyzed recrystallization at the atomic scale, and substantiate speculation regarding the role of defects controlling the dynamics of electron transfer and AE interaction at this important redox interface.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Visualizing the iron atom exchange front in the Fe(II)-catalyzed recrystallization of goethite by atom probe tomography

Taylor

Liu

Zhang

et al. 2019

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

View full text Add to dashboard Cite

show abstract

“…Specimen fracture and field‐induced deformation has therefore, to date, largely precluded routine atom probe analysis of soft materials . Notable exceptions include studies of ferritin clusters and molecules, mammalian and bacterial cells, and organic fibers in the chiton tooth …”

mentioning

confidence: 99%

Atom Probe Tomography for 3D Structural and Chemical Analysis of Individual Proteins

Sundell

Hulander

Pihl

et al. 2019

Small

View full text Add to dashboard Cite

Determination of the 3D structure of proteins and other biomolecules is a major goal in structural biology, to provide insights to their biological function. Such structures are historically unveiled experimentally by X‐ray crystallography or NMR spectroscopy, and in recent years using cryo‐electron microscopy. Here, a method for structural analysis of individual proteins on the sub‐nanometer scale using atom probe tomography is described. This technique offers a combination of high‐resolution analysis of biomolecules in 3D, and the chemical sensitivity of mass spectrometry. As a model protein, the well‐characterized antibody IgG is used. IgG is encapsulated in an amorphous solid silica matrix via a sol–gel process to provide the requisite support for atom probe analysis. The silica synthesis is tuned to resemble physiological conditions. The 3D reconstructions show good agreement with the protein databank IgG crystal structure. This suggests that the silica‐embedding strategy can open the field of atom probe tomography to the analysis of biological molecules. In addition to high‐resolution structural information, the technique may potentially provide chemical information on the atomic scale using isotopic labeling. It is envisaged that this method may constitute a useful complement to existing tools in structural biology, particularly for the examination of proteins with low propensity for crystallization.

show abstract

“…Moreover, we have found that metal ions strongly influence the conformation, the thermal stability, as well as mechanical properties of gelatin molecules. Although gelatin hydrogels as well as the modified hydrogels have been extensively studied, there are only a few reports on the influence of ions on the structure and mechanical properties of gelatin hydrogels …”

Section: Introductionmentioning

confidence: 99%

Ionic Dependence of Gelatin Hydrogel Architecture Explored Using Small and Very Small Angle Neutron Scattering Technique

Siglreitmeier

Debus

et al. 2018

Macromolecular Bioscience

View full text Add to dashboard Cite

The hierarchical structure of gelatin hydrogels mimics a natural extracellular matrix and provides an optimized microenvironment for the growth of 3D structured tissue analogs. In the presence of metal ions, gelatin hydrogels exhibit various mechanical properties that are correlated with the molecular interactions and the hierarchical structure. The structure and structural response of gelatin hydrogels to variation of gelatin concentration, pH, or addition of metal ions are explored by small and very small angle neutron scattering over broad length scales. The measurements of the hydrogels reveal the existence of a two‐level structure of colloid‐like large clusters and a 3D cage‐like gel network. In the presence of Fe3+ ions the hydrogels show a highly dense and stiff network, while Ca2+ ions have an opposite effect. The results provide important structural insight for improvement of the design of gelatin based hydrogels and are therefore suitable for various applications.

show abstract

Atom Probe Tomographic Mapping Directly Reveals the Atomic Distribution of Phosphorus in Resin Embedded Ferritin

Cited by 60 publications

References 36 publications

Visualizing the iron atom exchange front in the Fe(II)-catalyzed recrystallization of goethite by atom probe tomography

Visualizing the iron atom exchange front in the Fe(II)-catalyzed recrystallization of goethite by atom probe tomography

Atom Probe Tomography for 3D Structural and Chemical Analysis of Individual Proteins

Ionic Dependence of Gelatin Hydrogel Architecture Explored Using Small and Very Small Angle Neutron Scattering Technique

Contact Info

Product

Resources

About