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17 - Visualizing Macromolecules in Liquid at the Nanoscale

from Part II - Applications

Published online by Cambridge University Press:  22 December 2016

By
Andrew C. Demmert ,
Madeline J. Dukes ,
Elliot Pohlmann ,
Kaya Patel ,
A. Cameron Varano ,
Zhi Sheng ,
Sarah M. McDonald ,
Michael Spillman ,
Utkur Mirsaidov  and
Paul Matsudaira
...Show all authors
Edited by
Frances M. Ross
Frances M. Ross
Affiliation:
IBM T. J. Watson Research Center, New York
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Information
Liquid Cell Electron Microscopy , pp. 356 - 370
Publisher: Cambridge University Press
Print publication year: 2016

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References

De Carlo, S. and Harris, J. R., Negative staining and cryo-negative staining of macromolecules and viruses for TEM. Micron, 42 (2011), 117–131.Google Scholar
Dubochet, J. et al., Cryo-electron microscopy of vitrified specimens. Q. Rev. Biophys., 21 (1988), 129–228.CrossRefGoogle ScholarPubMed
Unwin, N. and Henderson, R., The structure of proteins in biological membranes. Sci. Am., 250 (1984), 78–94.CrossRefGoogle ScholarPubMed
Parsons, D. F., Matricardi, V. R., Moretz, R. C. and Turner, J. N., Electron microscopy and diffraction of wet unstained and unfixed biological objects. Adv. Biol. Med. Phys., 15 (1974), 161–270.CrossRefGoogle ScholarPubMed
Parsons, D. F., Structure of wet specimens in electron microscopy: improved environmental chambers make it possible to examine wet specimens easily. Science, 186 (1974), 407–414.Google Scholar
Dukes, M. J., Jacobs, B. W., Morgan, D. G., Hegde, H. and Kelly, D. F., Visualizing nanoparticle mobility in liquid at atomic resolution. Chem. Commun., 49 (2013), 3007–3009.Google Scholar
Kelly, D. F., Abeyrathne, P. D., Dukovski, D. and Walz, T., The Affinity Grid: a pre-fabricated EM grid for monolayer purification. J. Mol. Biol., 382 (2008), 423–433.CrossRefGoogle ScholarPubMed
Kelly, D. F., Dukovski, D. and Walz, T., A practical guide to the use of monolayer purification and affinity grids. Methods Enzymol., 481 (2010), 83–107.CrossRefGoogle Scholar
Degen, K., Dukes, M., Tanner, J. R. and Kelly, D. F., The development of affinity capture devices: a nanoscale purification platform for biological in situ transmission electron microscopy. RSC Adv., 2 (2012), 2408–2412.Google Scholar
Gilmore, B. L., Showalter, S. P., Dukes, M. J. et al., Visualizing viral assemblies in a nanoscale biosphere. Lab Chip, 13 (2013), 216–219.Google Scholar
Dukes, M. J., Thomas, R., Damiano, J. et al., Improved microchip design and application for in situ transmission electron microscopy of macromolecules. Microsc. Microanal., 20 (2014), 338–345.CrossRefGoogle ScholarPubMed
Pohlmann, E. S., Patel, K., Guo, S. et al., Real-time visualization of nanoparticles interacting with glioblastoma stem cells. Nano Lett., 15 (2015), 2329–2335.Google Scholar
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), L15–17.CrossRefGoogle Scholar
Ring, E. A., Peckys, D. B., Dukes, M. J., Baudoin, J. P. and de Jonge, N., Silicon nitride windows for electron microscopy of whole cells. J. Microsc. Oxford, 243 (2011), 273–283.CrossRefGoogle ScholarPubMed
Cameron Varano, A., Rahimi, A., Dukes, M. J. et al., Visualizing virus particle mobility in liquid at the nanoscale. Chem Commun., 51 (2015), 16176–16179.Google Scholar
Scheres, S. H., A Bayesian view on cryo-EM structure determination. J. Mol. Biol., 415 (2012), 406–418.Google Scholar
Zhang, X., Settembre, E., Xu, C. et al., Near-atomic resolution using electron cryomicroscopy and single-particle reconstruction. Proc. Natl. Acad. Sci. USA, 105 (2008), 1867–1872.CrossRefGoogle ScholarPubMed
Tilney, L. G., Actin filaments in the acrosomal reaction of Limulus sperm: motion generated by alterations in the packing of the filaments. J. Cell. Biol., 64 (1975), 289–310.CrossRefGoogle ScholarPubMed
Shin, J. H., Tam, B. K., Brau, R. R. et al., Force of an actin spring. Biophys. J., 92 (2007), 3729–3733.CrossRefGoogle ScholarPubMed
Wade, R. H., The temperature-dependence of radiation-damage in organic and biological materials. Ultramicroscopy, 14 (1984), 265–270.CrossRefGoogle Scholar
Leapman, R. D. and Sun, S. Q., Cryoelectron energy-loss spectroscopy: observations on vitrified hydrated specimens and radiation-damage. Ultramicroscopy, 59 (1995), 71–79.Google Scholar
Aronova, M. A., Sousa, A. A. and Leapman, R. D., EELS characterization of radiolytic products in frozen samples. Micron, 42 (2011), 252–256.Google Scholar
Yakovlev, S., Misra, M., Shi, S. and Libera, M., Specimen thickness dependence of hydrogen evolution during cryo-transmission electron microscopy of hydrated soft materials. J. Microsc. Oxford, 236 (2009), 174–179.CrossRefGoogle ScholarPubMed
Danev, R. and Nagayama, K, Transmission electron microscopy with Zernike phase plate. Ultramicroscopy, 88 (2001), 243–252.Google Scholar

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