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23 - Future Prospects for Biomolecular, Biomimetic, and Biomaterials Research Enabled by New Liquid Cell Electron Microscopy Techniques

from Part III - Prospects

Published online by Cambridge University Press:  22 December 2016

Frances M. Ross
Affiliation:
IBM T. J. Watson Research Center, New York
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Print publication year: 2016

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References

Stapels, D. A. C., Ramyar, K. X., Bischoff, M. et al., Staphylococcus aureus secretes a unique class of neutrophil serine protease inhibitors. Proc. Natl. Acad. Sci. USA, 111 (2014), 1318713192.CrossRefGoogle ScholarPubMed
Kendrew, J. C., Bodo, G., Dintzis, H. M. et al., A three-dimensional model of the myoglobin molecule obtained by X-ray analysis. Nature, 181 (1958), 662666.CrossRefGoogle ScholarPubMed
Frank, J., Single-particle imaging of macromolecules by cryo-electron microscopy. Annu. Rev. Biophys. Biomol. Struct., 31 (2002), 303319.CrossRefGoogle ScholarPubMed
Schmidt, A., Teeter, M., Weckert, E. and Lamzin, V. S., Crystal structure of small protein crambin at 0.48 Å resolution. Acta Crystallogr. Sect. F, 67 (2011), 424428.CrossRefGoogle ScholarPubMed
Bai, X. C., Fernandez, I. S., McMullan, G. and Scheres, S. H. W., Ribosome structures to near-atomic resolution from thirty thousand cryo-EM particles. eLife, 2 (2013), e00461.CrossRefGoogle ScholarPubMed
Bartesaghi, A., Matthies, D., Banerjee, S., Merk, A. and Subramaniam, S., Structure of beta-galactosidase at 3.2-angstrom resolution obtained by cryo-electron microscopy. Proc. Natl. Acad. Sci. USA, 111 (2014), 1170911714.CrossRefGoogle Scholar
Glaeser, R. M., Retrospective: Radiation damage and its associated “Information Limitations”. J. Struct. Biol., 163 (2008), 271276.CrossRefGoogle ScholarPubMed
Egerton, R. F., Control of radiation damage in the TEM. Ultramicroscopy, 127 (2013), 100108.CrossRefGoogle ScholarPubMed
Gilmore, B. L., Showalter, S. P., Dukes, M. J. et al., Visualizing viral assemblies in a nanoscale biosphere. Lab Chip, 13 (2013), 216219.CrossRefGoogle Scholar
Reimer, L. and Kohl, H., Transmission Electron Microscopy: Physics of Image Formation (New York: Springer, 2008).Google Scholar
Grogan, J. M., Schneider, N. M., Ross, F. M. and Bau, H. H., Bubble and pattern formation in liquid induced by an electron beam. Nano Lett., 14 (2014), 359364.CrossRefGoogle ScholarPubMed
Schneider, N. M., Norton, M. M., Mendel, B. J. et al., Electron-water interactions and implications for liquid cell electron microscopy. J. Phys. Chem. C, 118 (2014), 2237322382.CrossRefGoogle Scholar
Woehl, T. J., Jungjohann, K. L., Evans, J. E. et al., Experimental procedures to mitigate electron beam induced artifacts during in situ fluid imaging of nanomaterials. Ultramicroscopy, 127 (2013), 5363.CrossRefGoogle ScholarPubMed
Mirsaidov, U. M., Zheng, H., Casana, Y. and Matsudaira, P., Imaging protein structure in water at 2.7 nm resolution by transmission electron microscopy. Biophys. J., 102 (2012), L15L17.CrossRefGoogle Scholar
Evans, J. E. and Browning, N. D., Enabling direct nanoscale observations of biological reactions with dynamic TEM. Microscopy, 62 (2013), 147156.CrossRefGoogle ScholarPubMed
Jungjohann, K. L., Bliznakov, S., Sutter, P. W., Stach, E. A. and Sutter, E. A., In situ liquid cell electron microscopy of the solution growth of Au-Pd core-shell nanostructures. Nano Lett., 13 (2013), 29642970.CrossRefGoogle ScholarPubMed
Lowenstam, H. A. and Weiner, S., On Biomineralization (New York: Oxford University Press, 1989).CrossRefGoogle Scholar
Benzerara, K., Skouri-Panet, F., Li, J. H. et al., Intracellular Ca-carbonate biomineralization is widespread in cyanobacteria. Proc. Natl. Acad. Sci. USA, 111 (2014), 1093310938.CrossRefGoogle ScholarPubMed
Bazylinski, D. A., Synthesis of the bacterial magnetosome: the making of a magnetic personality. Int. Microbiol, 2 (1999), 7180.Google ScholarPubMed
Sumper, M. and Brunner, E., Learning from diatoms: nature’s tools for the production of nanostructured silica. Adv. Funct. Mater., 16 (2006), 1726.CrossRefGoogle Scholar
Woehl, T. J., Kashyap, S., Firlar, E. et al., Correlative electron and fluorescence microscopy of magnetotactic bacteria in liquid: toward in vivo imaging. Sci. Rep., 4 (2014), 6854.CrossRefGoogle ScholarPubMed
Arakaki, A., Webb, J. and Matsunaga, T., A novel protein tightly bound to bacterial magnetic particles in Magnetospirillum magneticum strain AMB-1. J. Biol. Chem., 278 (2003), 87458750.CrossRefGoogle ScholarPubMed
Poulsen, N., Sumper, M. and Kroger, N., Biosilica formation in diatoms: characterization of native silaffin-2 and its role in silica morphogenesis. Proc. Natl. Acad. Sci. USA, 100 (2003), 1207512080.CrossRefGoogle ScholarPubMed
Prozorov, T., Bazylinski, D. A., Mallapragada, S. K. and Prozorov, R., Novel magnetic nanomaterials inspired by magnetotactic bacteria: topical review. Mater. Sci. Eng. R., 74 (2013), 133172.CrossRefGoogle Scholar
Lang, C. and Schueler, D., Biomineralization of magnetosomes in bacteria: nanoparticles with potential applications. In Rehm, B., ed., Microbial Bionanotechnology (Wymondham, UK: Horizon Bioscience, 2006) pp. 107124.Google Scholar
Prozorov, T., Palo, P., Wang, L. et al., Cobalt ferrite nanocrystals: out-performing magnetotactic bacteria. ACS Nano, 1 (2007), 228233.CrossRefGoogle ScholarPubMed
Colfen, H. and Antonietti, M., Mesocrystals: inorganic superstructures made by highly parallel crystallization and controlled alignment. Angew. Chem. Int. Ed., 44 (2005), 55765591.CrossRefGoogle ScholarPubMed
Bazylinski, D. A., Garrattreed, A. J. and Frankel, R. B., Electron-microscopic studies of magnetosomes in magnetotactic bacteria. Microsc. Res. Tech., 27 (1994), 389401.CrossRefGoogle ScholarPubMed
Komeili, A., Li, Z., Newmana, D. K. and Jensen, G. J., Magnetosomes are cell membrane invaginations organized by the actin-like protein MamK. Science, 311 (2006), 242245.CrossRefGoogle ScholarPubMed
Pouget, E. M., Bomans, P. H. H., Goos, J. et al., The initial stages of template-controlled CaCO3 formation revealed by cryo-TEM. Science, 323 (2009), 14551458.CrossRefGoogle ScholarPubMed
Bazylinski, D. A. and Frankel, R. B., Magnetosome formation in prokaryotes. Nat. Rev. Micro., 2 (2004), 217230.CrossRefGoogle ScholarPubMed
Faivre, D. and Schüler, D., Magnetotactic bacteria and magnetosomes. Chem. Rev., 108 (2008), 48754898.CrossRefGoogle ScholarPubMed
Prozorov, T., Mallapragada, S. K., Narasimhan, B. et al., Protein-mediated synthesis of uniform superparamagnetic magnetite nanocrystals. Adv. Funct. Mater., 17 (2007), 951957.CrossRefGoogle Scholar
Epp, E. R., Weiss, H. and Santomasso, A., The oxygen effect in bacterial cells irradiated with high-intensity pulsed electrons. Rad. Res., 34 (1968), 320325.CrossRefGoogle ScholarPubMed
Komeili, A., Vali, H., Beveridge, T. J. and Newman, D. K., Magnetosome vesicles are present before magnetite formation, and MamA is required for their activation. Proc. Natl. Acad. Sci. USA, 101 (2004), 38393844.CrossRefGoogle ScholarPubMed
White, E. R., Singer, S. B., Augustyn, V. et al., In situ transmission electron microscopy of lead dendrites and lead ions in aqueous solution. ACS Nano, 6 (2012), 63086317.CrossRefGoogle ScholarPubMed
Kashyap, S., Woehl, T. J., Liu, X., Mallapragada, S. K. and Prozorov, T., Nucleation of iron oxide nanoparticles mediated by Mms6 protein in situ. ACS Nano, 8 (2014), 90979106.CrossRefGoogle ScholarPubMed
ISO/ASTM51540-09, USA, 2009. Standard Practices for Use of Radiochromic Liquid Dosimetry System, ASTM International, West Conshohocken, PA, USA.Google Scholar
Fiester, S. E., Helfinstine, S. L., Redfearn, J. C., Uribe, R. M. and Woolverton, C. J., Electron beam irradiation dose dependently damages the Bacillus spore coat and spore membrane. Int. J. Microbiol. (2012), 579593.CrossRefGoogle Scholar
Ward, G. D., Watson, I. A., Stewart-Tull, D. E. et al., Bactericidal action of high-power Nd:YAG laser light on Escherichia coli in saline suspension. J. Appl. Microbiol., 89 (2000), 517525.CrossRefGoogle ScholarPubMed
Nandakumar, K., Obika, H., Utsumi, A., Ooie, T. and Yano, T., Molecular level damages of low power pulsed laser radiation in a marine bacterium Pseudoalteromonas carrageenovora. Lett. Appl. Microbiol., 42 (2006), 521526.CrossRefGoogle Scholar
Tuszyn’ski, J. A., Portet, S., Dixon, J. M., Luxford, C. and Cantiello, H. F., Ionic wave propagation along actin filaments. Biophys. J., 86 (2004), 18901903.CrossRefGoogle Scholar
Cantiello, H. F., Patenaude, C. and Zaner, K., Osmotically induced electrical signals from actin filaments. Biophys. J., 59 (1991), 12841289.CrossRefGoogle ScholarPubMed
Merla, C., Paffi, A., Apollonio, F. et al., Microdosimetry for nanosecond pulsed electric field applications: a parametric study for a single cell. IEEE Trans. Biomed. Eng., 58 (2011), 12941302.CrossRefGoogle Scholar
Cowley, J. M., Twenty forms of electron holography. Ultramicroscopy, 41 (1992), 335348.CrossRefGoogle Scholar
Formanek, P., Lenk, A., Lichte, H. et al., Electron holography: applications to materials questions. Annu. Rev. Mater. Res., 37 (2007), 539588.Google Scholar
Dunin-Borkowski, R. E., McCartney, M. R., Kardynal, B. et al., Off-axis electron holography of exchange-biased CoFe/FeMn patterned nanostructures. J Appl. Phys., 90 (2001), 28992902.CrossRefGoogle Scholar
Simon, P., Lichte, H., Formanek, P. et al., Electron holography of biological samples. Micron, 39 (2008), 229256.CrossRefGoogle ScholarPubMed
Dunin-Borkowski, R. E., McCartney, M. R., Posfai, M. et al., Off-axis electron holography of magnetotactic bacteria: magnetic microstructure of strains MV-1 and MS-1. Eur. J. Mineral., 13 (2001), 671684.CrossRefGoogle Scholar
Kasama, T., Posfai, M., Chong, R. K. K. et al., Magnetic properties, microstructure, composition, and morphology of greigite nanocrystals in magnetotactic bacteria from electron holography and tomography. Am. Mineral., 91 (2006), 12161229.CrossRefGoogle Scholar
Simpson, E. T., Kasama, T., Posfai, M. et al., Magnetic induction mapping of magnetite chains in magnetotactic bacteria at room temperature and close to the Verwey transition using electron holography. J. Phys. Conf. Ser., 17 (2005), 108121.CrossRefGoogle Scholar
Longchamp, J. N., Latychevskaia, T., Escher, C. and Fink, H. W., Non-destructive imaging of an individual protein. Appl. Phys. Lett., 101 (2012), 093701.CrossRefGoogle Scholar
Kawasaki, T., Endo, J., Matsuda, T., Osakabe, N. and Tonomura, A., Applications of holographic interference electron microscopy to the observation of biological specimens. J. Electron Microsc., 35 (1986), 211214.Google Scholar
Pan, Y.-H., Sader, K., Powell, J. J. et al., 3D morphology of the human hepatic ferritin mineral core: new evidence for a subunit structure revealed by single particle analysis of HAADF-STEM images. J. Struct. Biol., 166 (2009), 2231.CrossRefGoogle ScholarPubMed
Lichte, H., Banzhof, H. and Huhle, R., Limitations in electron holography of magnetic microstructures. Proc. Int. Congr. Electr. Microsc., ICEM 14, Cancun, Mexico (1998), pp. 559–560.Google Scholar
Krack, M., Hohenberg, H., Kornowski, A. et al., Nanoparticle-loaded magnetophoretic vesicles. J. Am. Chem. Soc., 130 (2008), 73157320.CrossRefGoogle ScholarPubMed
Hopster, H. and Oepen, H. P. (eds.), Magnetic Microscopy of Nanostructures (Berlin: Springer, 2005).CrossRefGoogle Scholar
Eggeman, A. S., Petford-Long, A. K., Dobson, P. J. et al., Synthesis and characterization of silica encapsulated cobalt nanoparticles and nanoparticle chains. J. Magn. Magn. Mater., 301 (2006), 336342.CrossRefGoogle Scholar
Tanase, M. and Petford-Long, A. K., In situ TEM observation of magnetic materials. Microsc. Res. Tech., 72 (2009), 187196.CrossRefGoogle ScholarPubMed
Campbell, G. H., LaGrange, T. B., King, W. E. et al., The HCP to BCC phase transformation in Ti characterized by nanosecond electron microscopy. Solid-Solid Phase Transform. Inorg. Mater. 2005, Proc. Int. Conf., 2 (2005) 443–448.Google Scholar
Pankhurst, Q. A., Connolly, J., Jones, S. K. and Dobson, J., Applications of magnetic nanoparticles in biomedicine. J. Phys. D: Appl. Phys., 36 (2003), R167R181.CrossRefGoogle Scholar
Reiss, G. and Huetten, A., Magnetic nanoparticles: applications beyond data storage. Nat. Mater., 4 (2005), 725726.CrossRefGoogle ScholarPubMed
Förster, S., Amphiphilic block copolymers for templating applications. Top. Curr. Chem., 226 (2003), 128.CrossRefGoogle Scholar
Prozorov, T., Unpublished, 2013.CrossRefGoogle Scholar
Zhang, L., Song, S. I., Zheng, S. et al., Nontoxic poly(ethylene oxide phosphonamidate) hydrogels as templates for biomimetic mineralization of calcium carbonate and hydroxyapatite architectures. J. Mater. Sci., 48 (2013), 288298.CrossRefGoogle Scholar
Dobrunz, D., Toma, A. C., Tanner, P., Pfohl, T. and Palivan, C. G., Polymer nanoreactors with dual functionality: simultaneous detoxification of peroxynitrite and oxygen transport. Langmuir, 28 (2012), 1588915899.CrossRefGoogle ScholarPubMed
Tanner, P., Baumann, P., Enea, R. et al., Polymeric vesicles: from drug carriers to nanoreactors and artificial organelles. Acc. Chem. Res., 44 (2011), 10391049.CrossRefGoogle ScholarPubMed
Goswami, N., Saha, R. and Pal, S. K., Protein-assisted synthesis route of metal nanoparticles: exploration of key chemistry of the biomolecule. J. Nanopart. Res., 13 (2011), 54855495.CrossRefGoogle Scholar
Vriezema, D. M., Aragones, M. C., Elemans, J. A. A. W. et al., Self-assembled nanoreactors, Chem. Rev., 105 (2005), 14451489.CrossRefGoogle ScholarPubMed
Kashyap, S., Woehl, T., Valverde-Tercedor, C. et al., Visualization of iron-binding micelles in acidic recombinant biomineralization protein, MamC. J. Nanomater. (2014), 320124.CrossRefGoogle Scholar
Karlin, D. and Belshaw, R., Detecting remote sequence homology in disordered proteins: discovery of conserved motifs in the N-termini of Mononegavirales phosphoproteins. PLoS One, 7 (2012), e31719.CrossRefGoogle ScholarPubMed
Heyman, A., Medalsy, I., Bet Or, O. et al., Protein scaffold engineering towards tunable surface attachment. Angew. Chem. Int. Ed., 48 (2009), 92909294.CrossRefGoogle ScholarPubMed
Ghosh, P. S. and Hamilton, A. D., Noncovalent template-assisted mimicry of multiloop protein surfaces: assembling discontinuous and functional domains. J. Am. Chem. Soc., 134 (2012), 1320813211.CrossRefGoogle ScholarPubMed
Diao, J., Crystal structure of a super leucine zipper, an extended two-stranded super long coiled coil. Protein Sci., 19 (2010), 319326.CrossRefGoogle ScholarPubMed
Dedeo, M. T., Duderstadt, K. E., Berger, J. M. and Francis, M. B., Nanoscale protein assemblies from a circular permutant of the tobacco mosaic virus. Nano Lett., 10 (2010), 181186.CrossRefGoogle ScholarPubMed
Aniagyei, S. E., DuFort, C., Kao, C. C. and Dragnea, B., Self-assembly approaches to nanomaterial encapsulation in viral protein cages. J. Mater. Chem., 18 (2008), 37633774.CrossRefGoogle ScholarPubMed
Sun, J., DuFort, C., Daniel, M.-C. et al., Core-controlled polymorphism in virus-like particles. Proc. Natl. Acad. Sci. USA, 104 (2007), 13541359.CrossRefGoogle ScholarPubMed
Vatta, L. L., Sanderson, R. D. and Koch, K. R., Magnetic nanoparticles: properties and potential applications. Pure Appl. Chem., 78 (2006), 17931801.CrossRefGoogle Scholar
Ai, H., Flask, C., Weinberg, B. et al., Magnetite-loaded polymeric micelles as ultrasensitive magnetic-resonance probes. Adv. Mater., 17 (2005), 19491952.CrossRefGoogle Scholar
Berry, C. C. and Curtis, A. S. G., Functionalisation of magnetic nanoparticles for applications in biomedicine. J. Phys. D: Appl. Phys., 36 (2003), R198R206.CrossRefGoogle Scholar
Chiancone, E., Ceci, P., Ilari, A., Ribacchi, F. and Stefanini, S., Iron and proteins for iron storage and detoxification. BioMetals, 17 (2004), 197202.CrossRefGoogle ScholarPubMed
Busch, A. P., Rhinow, D., Yang, F. et al., Site-selective biomineralization of native biological membranes. J. Mater. Chem. B, 2 (2014), 69246930.CrossRefGoogle ScholarPubMed
Baumgartner, J., Morin, G., Menguy, N. et al., Magnetotactic bacteria form magnetite from a phosphate-rich ferric hydroxide via nanometric ferric (oxyhydr)oxide intermediates. Proc. Natl. Acad. Sci. USA, 110 (2013), 1488314888.CrossRefGoogle ScholarPubMed
Baumgartner, J. and Faivre, D., Magnetite biomineralization in bacteria. Prog. Mol. Subcell. Biol., 52 (2011), 327.CrossRefGoogle ScholarPubMed
Penn, R. L. and Banfield, J. F., Imperfect oriented attachment: dislocation generation in defect-free nanocrystals. Science, 281 (1998), 969971.CrossRefGoogle ScholarPubMed
Gao, B., Arya, G. and Tao, A. R., Self-orienting nanocubes for the assembly of plasmonic nanojunctions. Nat. Nanotechnol., 7 (2012), 433437.CrossRefGoogle ScholarPubMed
Nakagawa, Y., Kageyama, H., Oaki, Y. and Imai, H., Direction control of oriented self-assembly for 1D, 2D, and 3D microarrays of anisotropic rectangular nanoblocks. J. Am. Chem. Soc., 136 (2014), 37163719.CrossRefGoogle ScholarPubMed
Song, R. Q. and Colfen, H., Mesocrystals-ordered nanoparticle superstructures. Adv. Mater., 22 (2010), 13011330.CrossRefGoogle ScholarPubMed
Sun, B. L., Wen, M., Wu, Q. S. and Peng, J., Oriented growth and assembly of Ag@C@Co pentagonalprism nanocables and their highly active selected catalysis along the edges for dehydrogenation. Adv. Funct. Mater., 22 (2012), 28602866.CrossRefGoogle Scholar
Ihli, J., Bots, P., Kulak, A., Benning, L. G. and Meldrum, F. C., Elucidating mechanisms of diffusion-based calcium carbonate synthesis leads to controlled mesocrystal formation. Adv. Funct. Mater., 23 (2013), 19651973.CrossRefGoogle Scholar
Niederberger, M. and Colfen, H., Oriented attachment and mesocrystals: non-classical crystallization mechanisms based on nanoparticle assembly. Phys. Chem. Chem. Phys., 8 (2006), 32713287.CrossRefGoogle ScholarPubMed
Frandsen, C., Legg, B. A., Comolli, L. R. et al., Aggregation-induced growth and transformation of beta-FeOOH nanorods to micron-sized alpha-Fe2O3 spindles. CrystEngComm, 16 (2014), 14511458.CrossRefGoogle Scholar
Wang, Y., DePrince, A. E., Gray, S. K., Lin, X. M. and Pelton, M., Solvent-mediated end-to-end assembly of gold nanorods. J. Phys. Chem. Lett., 1 (2010), 26922698.CrossRefGoogle ScholarPubMed
Colfen, H. and Antonietti, M., Mesocrystals and Nonclassical Crystallization (Chichester, UK: Wiley, 2008).CrossRefGoogle Scholar
Woehl, T. J. and Prozorov, T., The mechanisms for nanoparticle surface diffusion and chain self-assembly determined from real-time nanoscale kinetics in liquid. J. Phys. Chem. C, 119 (2015), 2126121269.CrossRefGoogle Scholar
Burrows, N. D., Hale, C. R. H. and Penn, R. L., Effect of ionic strength on the kinetics of crystal growth by oriented aggregation. Cryst. Growth Des., 12 (2012), 47874797.CrossRefGoogle Scholar
Penn, R. L. and Soltis, J. A., Characterizing crystal growth by oriented aggregation. CrystEngComm, 16 (2014), 14091418.CrossRefGoogle Scholar
Ahmed, W., Laarman, R. P. B., Hellenthal, C. et al., Dipole directed ring assembly of Ni-coated Au-nanorods. Chem. Commun., 46 (2010), 67116713.CrossRefGoogle ScholarPubMed
Chai, J., Liao, X., Giam, L. R. and Mirkin, C. A., Nanoreactors for studying single nanoparticle coarsening. J. Am. Chem. Soc., 134 (2012), 158161.CrossRefGoogle ScholarPubMed
Yang, M. X., Chen, G., Zhao, Y. F. et al., Mechanistic investigation into the spontaneous linear assembly of gold nanospheres. Phys. Chem. Chem. Phys., 12 (2010), 1185011860.CrossRefGoogle ScholarPubMed
Park, J., Zheng, H., Lee, W. C. et al., Direct observation of nanoparticle superlattice formation by using liquid cell transmission electron microscopy. ACS Nano, 6 (2012), 20782085.CrossRefGoogle ScholarPubMed
Park, C., Woehl, T. J., Evans, J. E. and Browning, N. D., Minimum cost multi-way data association for optimizing multitarget tracking of interacting objects, pattern analysis and machine intelligence. IEEE Trans. Pattern Anal. Mach. Intell., 37 (2014), 611624.CrossRefGoogle Scholar
Li, D. S., Nielsen, M. H., Lee, J. R. I. et al., Direction-specific interactions control crystal growth by oriented attachment. Science, 336 (2012), 10141018.CrossRefGoogle ScholarPubMed
Yuk, J. M., Park, J., Ercius, P. et al., High-resolution EM of colloidal nanocrystal growth using graphene liquid cells. Science, 336 (2012), 6164.CrossRefGoogle ScholarPubMed
Liao, H. G., Zherebetskyy, D., Xin, H. L. et al., Facet development during platinum nanocube growth. Science, 345 (2014), 916919.CrossRefGoogle ScholarPubMed

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