DOI: 10.1038/srep07084. Self-assembled monolayers improve protein distribution on holey carbon cryo-EM supports

Self-assembled monolayers improve protein distribution on holey carbon cryo-EM supports

10.1038/srep07084

Crossref journal-article

Springer Science and Business Media LLC

Scientific Reports (297)

Bibliography

Meyerson, J. R., Rao, P., Kumar, J., Chittori, S., Banerjee, S., Pierson, J., Mayer, M. L., & Subramaniam, S. (2014). Self-assembled monolayers improve protein distribution on holey carbon cryo-EM supports. Scientific Reports, 4(1).

Authors 8

Joel R. Meyerson (first)
Prashant Rao (additional)
Janesh Kumar (additional)
Sagar Chittori (additional)
Soojay Banerjee (additional)
Jason Pierson (additional)
Mark L. Mayer (additional)
Sriram Subramaniam (additional)

References 20 Referenced 91

Patwardhan, A. et al. Data management challenges in three-dimensional EM. Nat Struct Mol Biol 19, 1203–1207 (2012). (10.1038/nsmb.2426) / Nat Struct Mol Biol by A Patwardhan (2012)
Bartesaghi, A., Matthies, D., Banerjee, S., Merk, A. & Subramaniam, S. Structure of beta-galactosidase at 3.2-A resolution obtained by cryo-electron microscopy. Proc Natl Acad Sci U S A 111, 11709–11714 (2014). (10.1073/pnas.1402809111) / Proc Natl Acad Sci U S A by A Bartesaghi (2014)
Liao, M., Cao, E., Julius, D. & Cheng, Y. Structure of the TRPV1 ion channel determined by electron cryo-microscopy. Nature 504, 107–112 (2013). (10.1038/nature12822) / Nature by M Liao (2013)
Dubochet, J. et al. Cryo-electron microscopy of vitrified specimens. Q Rev Biophys 21, 129–228 (1988). (10.1017/S0033583500004297) / Q Rev Biophys by J Dubochet (1988)
Subramaniam, S., Gerstein, M., Oesterhelt, D. & Henderson, R. Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin. EMBO J 12, 1–8 (1993). (10.1002/j.1460-2075.1993.tb05625.x) / EMBO J by S Subramaniam (1993)
Pantelic, R. S., Suk, J. W., Hao, Y., Ruoff, R. S. & Stahlberg, H. Oxidative doping renders graphene hydrophilic, facilitating its use as a support in biological TEM. Nano Lett 11, 4319–4323 (2011). (10.1021/nl202386p) / Nano Lett by RS Pantelic (2011)
Rhinow, D. et al. Energy-filtered transmission electron microscopy of biological samples on highly transparent carbon nanomembranes. Ultramicroscopy 111, 342–349 (2011). (10.1016/j.ultramic.2011.01.028) / Ultramicroscopy by D Rhinow (2011)
Russo, C. J. & Passmore, L. A. Controlling protein adsorption on graphene for cryo-EM using low-energy hydrogen plasmas. Nat Methods 11, 649–652 (2014). (10.1038/nmeth.2931) / Nat Methods by CJ Russo (2014)
Yoshioka, C., Carragher, B. & Potter, C. S. Cryomesh: a new substrate for cryo-electron microscopy. Microsc Microanal 16, 43–53 (2010). (10.1017/S1431927609991310) / Microsc Microanal by C Yoshioka (2010)
Rhinow, D. & Kuhlbrandt, W. Electron cryo-microscopy of biological specimens on conductive titanium-silicon metal glass films. Ultramicroscopy 108, 698–705 (2008). (10.1016/j.ultramic.2007.11.005) / Ultramicroscopy by D Rhinow (2008)
Jain, T., Sheehan, P., Crum, J., Carragher, B. & Potter, C. S. Spotiton: a prototype for an integrated inkjet dispense and vitrification system for cryo-TEM. J Struct Biol 179, 68–75 (2012). (10.1016/j.jsb.2012.04.020) / J Struct Biol by T Jain (2012)
Liu, Y., Meng, X. & Liu, Z. Deformed grids for single-particle cryo-electron microscopy of specimens exhibiting a preferred orientation. J Struct Biol 182, 255–258 (2013). (10.1016/j.jsb.2013.03.005) / J Struct Biol by Y Liu (2013)
Kelly, D. F., Dukovski, D. & Walz, T. A practical guide to the use of monolayer purification and affinity grids. Methods Enzymol 481, 83–107 (2010). (10.1016/S0076-6879(10)81004-3) / Methods Enzymol by DF Kelly (2010)
Quispe, J. et al. An improved holey carbon film for cryo-electron microscopy. Microsc Microanal 13, 365–371 (2007). (10.1017/S1431927607070791) / Microsc Microanal by J Quispe (2007)
Schauder, D. M. et al. Glutamate receptor desensitization is mediated by changes in quaternary structure of the ligand binding domain. Proc Natl Acad Sci U S A (2013). (10.1016/j.bpj.2012.11.1953)
Prime, K. L. & Whitesides, G. M. Self-assembled organic monolayers: model systems for studying adsorption of proteins at surfaces. Science 252, 1164–1167 (1991). (10.1126/science.252.5009.1164) / Science by KL Prime (1991)
Cheung, M. et al. A method to achieve homogeneous dispersion of large transmembrane complexes within the holes of carbon films for electron cryomicroscopy. J Struct Biol (2013). (10.1016/j.jsb.2013.01.004)
Suh, K. Y. & Jon, S. Control over wettability of polyethylene glycol surfaces using capillary lithography. Langmuir 21, 6836–6841 (2005). (10.1021/la050878+) / Langmuir by KY Suh (2005)
Meyerson, J. R. et al. Structural mechanism of glutamate receptor activation and desensitization. Nature 514, 328–334 (2014). (10.1038/nature13603) / Nature by JR Meyerson (2014)
Li, X. et al. Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM. Nat Methods 10, 584–590 (2013). (10.1038/nmeth.2472) / Nat Methods by X Li (2013)

Dates

Type	When
Created	10 years, 9 months ago (Nov. 18, 2014, 6:59 a.m.)
Deposited	2 years, 7 months ago (Jan. 6, 2023, 12:59 a.m.)
Indexed	1 month, 1 week ago (July 14, 2025, 11:22 p.m.)
Issued	10 years, 9 months ago (Nov. 18, 2014)
Published	10 years, 9 months ago (Nov. 18, 2014)
Published Online	10 years, 9 months ago (Nov. 18, 2014)

Funders 0

None

BibTeX

@article{Meyerson_2014, title={Self-assembled monolayers improve protein distribution on holey carbon cryo-EM supports}, volume={4}, ISSN={2045-2322}, url={http://dx.doi.org/10.1038/srep07084}, DOI={10.1038/srep07084}, number={1}, journal={Scientific Reports}, publisher={Springer Science and Business Media LLC}, author={Meyerson, Joel R. and Rao, Prashant and Kumar, Janesh and Chittori, Sagar and Banerjee, Soojay and Pierson, Jason and Mayer, Mark L. and Subramaniam, Sriram}, year={2014}, month=nov }

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