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Recent advances in new technologies and applications for molecular TEM.

Journal of structural biology

Carragher B, Potter CS.
PMID: 26534727
J Struct Biol. 2015 Nov;192(2):145. doi: 10.1016/j.jsb.2015.10.013.

No abstract available.

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Carragher B, Potter CS. Recent advances in new technologies and applications for molecular TEM. J Struct Biol. 2015;192(2):145doi: 10.1016/j.jsb.2015.10.013.
Carragher, B., & Potter, C. S. (2015). Recent advances in new technologies and applications for molecular TEM. Journal of structural biology, 192(2), 145. https://doi.org/10.1016/j.jsb.2015.10.013
Carragher, Bridget, and Potter, Clinton S. "Recent advances in new technologies and applications for molecular TEM." Journal of structural biology vol. 192,2 (2015): 145. doi: https://doi.org/10.1016/j.jsb.2015.10.013
Carragher B, Potter CS. Recent advances in new technologies and applications for molecular TEM. J Struct Biol. 2015 Nov;192(2):145. doi: 10.1016/j.jsb.2015.10.013. PMID: 26534727.
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Keratin intermediate filaments: differences in the sequences of the Type I and Type II chains explain the origin of the stability of an enzyme-resistant four-chain fragment.

Journal of structural biology

Fraser RD, Parry DA.
PMID: 24384118
J Struct Biol. 2014 Mar;185(3):317-26. doi: 10.1016/j.jsb.2013.12.012. Epub 2013 Dec 30.

Previous studies have shown that a strong interaction exists between oppositely directed 1B molecular segments in the intermediate filaments of trichocyte keratins. A similar interaction has been identified as having a significant role in the formation of unit-length filaments,...

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Fraser RD, Parry DA. Keratin intermediate filaments: differences in the sequences of the Type I and Type II chains explain the origin of the stability of an enzyme-resistant four-chain fragment. J Struct Biol. 2013;185(3):317-26doi: 10.1016/j.jsb.2013.12.012.
Fraser, R. D., & Parry, D. A. (2014). Keratin intermediate filaments: differences in the sequences of the Type I and Type II chains explain the origin of the stability of an enzyme-resistant four-chain fragment. Journal of structural biology, 185(3), 317-26. https://doi.org/10.1016/j.jsb.2013.12.012
Fraser, R D Bruce, and Parry, David A D. "Keratin intermediate filaments: differences in the sequences of the Type I and Type II chains explain the origin of the stability of an enzyme-resistant four-chain fragment." Journal of structural biology vol. 185,3 (2014): 317-26. doi: https://doi.org/10.1016/j.jsb.2013.12.012
Fraser RD, Parry DA. Keratin intermediate filaments: differences in the sequences of the Type I and Type II chains explain the origin of the stability of an enzyme-resistant four-chain fragment. J Struct Biol. 2014 Mar;185(3):317-26. doi: 10.1016/j.jsb.2013.12.012. Epub 2013 Dec 30. PMID: 24384118.
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Reprint of: keratin intermediate filaments: differences in the sequences of the Type I and Type II chains explain the origin of the stability of an enzyme-resistant four-chain fragment.

Journal of structural biology

Fraser RD, Parry DA.
PMID: 24861529
J Struct Biol. 2014 Jun;186(3):481-90. doi: 10.1016/j.jsb.2014.05.005. Epub 2014 May 23.

Previous studies have shown that a strong interaction exists between oppositely directed 1B molecular segments in the intermediate filaments of trichocyte keratins. A similar interaction has been identified as having a significant role in the formation of unit-length filaments,...

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Fraser RD, Parry DA. Reprint of: keratin intermediate filaments: differences in the sequences of the Type I and Type II chains explain the origin of the stability of an enzyme-resistant four-chain fragment. J Struct Biol. 2014;186(3):481-90doi: 10.1016/j.jsb.2014.05.005.
Fraser, R. D., & Parry, D. A. (2014). Reprint of: keratin intermediate filaments: differences in the sequences of the Type I and Type II chains explain the origin of the stability of an enzyme-resistant four-chain fragment. Journal of structural biology, 186(3), 481-90. https://doi.org/10.1016/j.jsb.2014.05.005
Fraser, R D Bruce, and Parry, David A D. "Reprint of: keratin intermediate filaments: differences in the sequences of the Type I and Type II chains explain the origin of the stability of an enzyme-resistant four-chain fragment." Journal of structural biology vol. 186,3 (2014): 481-90. doi: https://doi.org/10.1016/j.jsb.2014.05.005
Fraser RD, Parry DA. Reprint of: keratin intermediate filaments: differences in the sequences of the Type I and Type II chains explain the origin of the stability of an enzyme-resistant four-chain fragment. J Struct Biol. 2014 Jun;186(3):481-90. doi: 10.1016/j.jsb.2014.05.005. Epub 2014 May 23. PMID: 24861529.
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Reprint of "Generation of ribosome nascent chain complexes for structural and functional studies" [J. Struct. Biol. 158 (2007) 463-471].

Journal of structural biology

Schaffitzel C, Ban N.
PMID: 17660065
J Struct Biol. 2007 Aug;159(2):302-10. doi: 10.1016/S1047-8477(07)00167-0.

Biochemical and structural studies of co-translational folding, targeting and translocation depend on an efficient methodology to prepare ribosome nascent chain complexes (RNCs). Here we present our approach for the generation of homogenous and stable RNCs involving in vitro translation...

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Schaffitzel C, Ban N. Reprint of "Generation of ribosome nascent chain complexes for structural and functional studies" [J. Struct. Biol. 158 (2007) 463-471]. J Struct Biol. 2007;159(2):302-10doi: 10.1016/S1047-8477(07)00167-0.
Schaffitzel, C., & Ban, N. (2007). Reprint of "Generation of ribosome nascent chain complexes for structural and functional studies" [J. Struct. Biol. 158 (2007) 463-471]. Journal of structural biology, 159(2), 302-10. https://doi.org/10.1016/S1047-8477(07)00167-0
Schaffitzel, Christiane, and Ban, Nenad. "Reprint of "Generation of ribosome nascent chain complexes for structural and functional studies" [J. Struct. Biol. 158 (2007) 463-471]." Journal of structural biology vol. 159,2 (2007): 302-10. doi: https://doi.org/10.1016/S1047-8477(07)00167-0
Schaffitzel C, Ban N. Reprint of "Generation of ribosome nascent chain complexes for structural and functional studies" [J. Struct. Biol. 158 (2007) 463-471]. J Struct Biol. 2007 Aug;159(2):302-10. doi: 10.1016/S1047-8477(07)00167-0. PMID: 17660065.
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Reprint of "Three-dimensional elemental mapping of phosphorus by quantitative electron spectroscopic tomography (QuEST)" [J. Struct. Biol. 160 (2007) 35-48].

Journal of structural biology

Aronova MA, Kim YC, Harmon R, Sousa AA, Zhang G, Leapman RD.
PMID: 18342742
J Struct Biol. 2008 Mar;161(3):322-35. doi: 10.1016/S1047-8477(08)00062-2.

We describe the development of quantitative electron spectroscopic tomography (QuEST), which provides 3-D distributions of elements on a nanometer scale. Specifically, it is shown that QuEST can be applied to map the distribution of phosphorus in unstained sections of...

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Aronova MA, Kim YC, Harmon R, et al. Reprint of "Three-dimensional elemental mapping of phosphorus by quantitative electron spectroscopic tomography (QuEST)" [J. Struct. Biol. 160 (2007) 35-48]. J Struct Biol. 2008;161(3):322-35doi: 10.1016/S1047-8477(08)00062-2.
Aronova, M. A., Kim, Y. C., Harmon, R., Sousa, A. A., Zhang, G., & Leapman, R. D. (2008). Reprint of "Three-dimensional elemental mapping of phosphorus by quantitative electron spectroscopic tomography (QuEST)" [J. Struct. Biol. 160 (2007) 35-48]. Journal of structural biology, 161(3), 322-35. https://doi.org/10.1016/S1047-8477(08)00062-2
Aronova, M A, et al. "Reprint of "Three-dimensional elemental mapping of phosphorus by quantitative electron spectroscopic tomography (QuEST)" [J. Struct. Biol. 160 (2007) 35-48]." Journal of structural biology vol. 161,3 (2008): 322-35. doi: https://doi.org/10.1016/S1047-8477(08)00062-2
Aronova MA, Kim YC, Harmon R, Sousa AA, Zhang G, Leapman RD. Reprint of "Three-dimensional elemental mapping of phosphorus by quantitative electron spectroscopic tomography (QuEST)" [J. Struct. Biol. 160 (2007) 35-48]. J Struct Biol. 2008 Mar;161(3):322-35. doi: 10.1016/S1047-8477(08)00062-2. PMID: 18342742.
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Reprint of "On the feasibility of visualizing ultrasmall gold labels in biological specimens by STEM tomography" [J. Struct. Biol. 159 (2007) 507-522].

Journal of structural biology

Sousa AA, Aronova MA, Kim YC, Dorward LM, Zhang G, Leapman RD.
PMID: 18342743
J Struct Biol. 2008 Mar;161(3):336-51. doi: 10.1016/S1047-8477(08)00063-4.

Labeling with heavy atom clusters attached to antibody fragments is an attractive technique for determining the 3D distribution of specific proteins in cells using electron tomography. However, the small size of the labels makes them very difficult to detect...

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Sousa AA, Aronova MA, Kim YC, et al. Reprint of "On the feasibility of visualizing ultrasmall gold labels in biological specimens by STEM tomography" [J. Struct. Biol. 159 (2007) 507-522]. J Struct Biol. 2008;161(3):336-51doi: 10.1016/S1047-8477(08)00063-4.
Sousa, A. A., Aronova, M. A., Kim, Y. C., Dorward, L. M., Zhang, G., & Leapman, R. D. (2008). Reprint of "On the feasibility of visualizing ultrasmall gold labels in biological specimens by STEM tomography" [J. Struct. Biol. 159 (2007) 507-522]. Journal of structural biology, 161(3), 336-51. https://doi.org/10.1016/S1047-8477(08)00063-4
Sousa, A A, et al. "Reprint of "On the feasibility of visualizing ultrasmall gold labels in biological specimens by STEM tomography" [J. Struct. Biol. 159 (2007) 507-522]." Journal of structural biology vol. 161,3 (2008): 336-51. doi: https://doi.org/10.1016/S1047-8477(08)00063-4
Sousa AA, Aronova MA, Kim YC, Dorward LM, Zhang G, Leapman RD. Reprint of "On the feasibility of visualizing ultrasmall gold labels in biological specimens by STEM tomography" [J. Struct. Biol. 159 (2007) 507-522]. J Struct Biol. 2008 Mar;161(3):336-51. doi: 10.1016/S1047-8477(08)00063-4. PMID: 18342743.
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Practical performance evaluation of a 10k × 10k CCD for electron cryo-microscopy.

Journal of structural biology

Bammes BE, Rochat RH, Jakana J, Chiu W.
PMID: 21619932
J Struct Biol. 2011 Sep;175(3):384-93. doi: 10.1016/j.jsb.2011.05.012. Epub 2011 May 17.

Electron cryo-microscopy (cryo-EM) images are commonly collected using either charge-coupled devices (CCD) or photographic film. Both film and the current generation of 16 megapixel (4k × 4k) CCD cameras have yielded high-resolution structures. Yet, despite the many advantages of...

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Bammes BE, Rochat RH, Jakana J, et al. Practical performance evaluation of a 10k × 10k CCD for electron cryo-microscopy. J Struct Biol. 2011;175(3):384-93doi: 10.1016/j.jsb.2011.05.012.
Bammes, B. E., Rochat, R. H., Jakana, J., & Chiu, W. (2011). Practical performance evaluation of a 10k × 10k CCD for electron cryo-microscopy. Journal of structural biology, 175(3), 384-93. https://doi.org/10.1016/j.jsb.2011.05.012
Bammes, Benjamin E, et al. "Practical performance evaluation of a 10k × 10k CCD for electron cryo-microscopy." Journal of structural biology vol. 175,3 (2011): 384-93. doi: https://doi.org/10.1016/j.jsb.2011.05.012
Bammes BE, Rochat RH, Jakana J, Chiu W. Practical performance evaluation of a 10k × 10k CCD for electron cryo-microscopy. J Struct Biol. 2011 Sep;175(3):384-93. doi: 10.1016/j.jsb.2011.05.012. Epub 2011 May 17. PMID: 21619932; PMCID: PMC3150461.
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Contrast transfer function correction applied to cryo-electron tomography and sub-tomogram averaging.

Journal of structural biology

Zanetti G, Riches JD, Fuller SD, Briggs JA.
PMID: 19666126
J Struct Biol. 2009 Nov;168(2):305-12. doi: 10.1016/j.jsb.2009.08.002. Epub 2009 Aug 08.

Cryo-electron tomography together with averaging of sub-tomograms containing identical particles can reveal the structure of proteins or protein complexes in their native environment. The resolution of this technique is limited by the contrast transfer function (CTF) of the microscope....

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Zanetti G, Riches JD, Fuller SD, et al. Contrast transfer function correction applied to cryo-electron tomography and sub-tomogram averaging. J Struct Biol. 2009;168(2):305-12doi: 10.1016/j.jsb.2009.08.002.
Zanetti, G., Riches, J. D., Fuller, S. D., & Briggs, J. A. (2009). Contrast transfer function correction applied to cryo-electron tomography and sub-tomogram averaging. Journal of structural biology, 168(2), 305-12. https://doi.org/10.1016/j.jsb.2009.08.002
Zanetti, Giulia, et al. "Contrast transfer function correction applied to cryo-electron tomography and sub-tomogram averaging." Journal of structural biology vol. 168,2 (2009): 305-12. doi: https://doi.org/10.1016/j.jsb.2009.08.002
Zanetti G, Riches JD, Fuller SD, Briggs JA. Contrast transfer function correction applied to cryo-electron tomography and sub-tomogram averaging. J Struct Biol. 2009 Nov;168(2):305-12. doi: 10.1016/j.jsb.2009.08.002. Epub 2009 Aug 08. PMID: 19666126; PMCID: PMC2806944.
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WITHDRAWN: Intrinsic molecular characteristics of inhibiting STAT3 activation and dimerization through targeting the phosphotyrosine binding site within the SH2 domain-A molecular dynamics study.

Journal of structural biology

Fan Y, Kong R, Tweardy DJ, Wong ST.
PMID: 23428430
J Struct Biol. 2013 Feb 18; doi: 10.1016/j.jsb.2013.02.005. Epub 2013 Feb 18.

This article has been withdrawn at the request of the author(s) and/or editor. The Publisher apologizes for any inconvenience this may cause. The full Elsevier Policy on Article Withdrawal can be found at http://www.elsevier.com/locate/withdrawalpolicy.

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Fan Y, Kong R, Tweardy DJ, et al. WITHDRAWN: Intrinsic molecular characteristics of inhibiting STAT3 activation and dimerization through targeting the phosphotyrosine binding site within the SH2 domain-A molecular dynamics study. J Struct Biol. 2013;doi: 10.1016/j.jsb.2013.02.005.
Fan, Y., Kong, R., Tweardy, D. J., & Wong, S. T. (2013). WITHDRAWN: Intrinsic molecular characteristics of inhibiting STAT3 activation and dimerization through targeting the phosphotyrosine binding site within the SH2 domain-A molecular dynamics study. Journal of structural biology, . https://doi.org/10.1016/j.jsb.2013.02.005
Fan, Yubo, et al. "WITHDRAWN: Intrinsic molecular characteristics of inhibiting STAT3 activation and dimerization through targeting the phosphotyrosine binding site within the SH2 domain-A molecular dynamics study." Journal of structural biology vol. (2013). doi: https://doi.org/10.1016/j.jsb.2013.02.005
Fan Y, Kong R, Tweardy DJ, Wong ST. WITHDRAWN: Intrinsic molecular characteristics of inhibiting STAT3 activation and dimerization through targeting the phosphotyrosine binding site within the SH2 domain-A molecular dynamics study. J Struct Biol. 2013 Feb 18; doi: 10.1016/j.jsb.2013.02.005. Epub 2013 Feb 18. PMID: 23428430.
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The DNA-binding mechanism of the TCS response regulator ArlR from Staphylococcus aureus.

Journal of structural biology

Yan H, Wang Q, Teng M, Li X.
PMID: 31520693
J Struct Biol. 2019 Dec 01;208(3):107388. doi: 10.1016/j.jsb.2019.09.005. Epub 2019 Sep 11.

ArlRS is an essential two-component system in Staphylococcus aureus that regulates the transcription of virulence factors and participate in numerous pathogenic and symbiotic processes. In this work, we identified different DNA binding properties and oligomerization states among the DNA-binding...

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Yan H, Wang Q, Teng M, et al. The DNA-binding mechanism of the TCS response regulator ArlR from Staphylococcus aureus. J Struct Biol. 2019;208(3):107388doi: 10.1016/j.jsb.2019.09.005.
Yan, H., Wang, Q., Teng, M., & Li, X. (2019). The DNA-binding mechanism of the TCS response regulator ArlR from Staphylococcus aureus. Journal of structural biology, 208(3), 107388. https://doi.org/10.1016/j.jsb.2019.09.005
Yan, Hui, et al. "The DNA-binding mechanism of the TCS response regulator ArlR from Staphylococcus aureus." Journal of structural biology vol. 208,3 (2019): 107388. doi: https://doi.org/10.1016/j.jsb.2019.09.005
Yan H, Wang Q, Teng M, Li X. The DNA-binding mechanism of the TCS response regulator ArlR from Staphylococcus aureus. J Struct Biol. 2019 Dec 01;208(3):107388. doi: 10.1016/j.jsb.2019.09.005. Epub 2019 Sep 11. PMID: 31520693.
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Erratum to "A new cryo-EM system for single particle analysis" [J. Struct. Biol. 207 (1) (2019) 40-48].

Journal of structural biology

Hamaguchi T, Maki-Yonekura S, Naitow H, Matsuura Y, Ishikawa T, Yonekura K.
PMID: 32622787
J Struct Biol. 2020 Sep 01;211(3):107558. doi: 10.1016/j.jsb.2020.107558. Epub 2020 Jul 01.

No abstract available.

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Hamaguchi T, Maki-Yonekura S, Naitow H, et al. Erratum to "A new cryo-EM system for single particle analysis" [J. Struct. Biol. 207 (1) (2019) 40-48]. J Struct Biol. 2020;211(3):107558doi: 10.1016/j.jsb.2020.107558.
Hamaguchi, T., Maki-Yonekura, S., Naitow, H., Matsuura, Y., Ishikawa, T., & Yonekura, K. (2020). Erratum to "A new cryo-EM system for single particle analysis" [J. Struct. Biol. 207 (1) (2019) 40-48]. Journal of structural biology, 211(3), 107558. https://doi.org/10.1016/j.jsb.2020.107558
Hamaguchi, Tasuku, et al. "Erratum to "A new cryo-EM system for single particle analysis" [J. Struct. Biol. 207 (1) (2019) 40-48]." Journal of structural biology vol. 211,3 (2020): 107558. doi: https://doi.org/10.1016/j.jsb.2020.107558
Hamaguchi T, Maki-Yonekura S, Naitow H, Matsuura Y, Ishikawa T, Yonekura K. Erratum to "A new cryo-EM system for single particle analysis" [J. Struct. Biol. 207 (1) (2019) 40-48]. J Struct Biol. 2020 Sep 01;211(3):107558. doi: 10.1016/j.jsb.2020.107558. Epub 2020 Jul 01. PMID: 32622787.
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3D mapping of native extracellular matrix reveals cellular responses to the microenvironment.

Journal of structural biology: X

Lansky Z, Mutsafi Y, Houben L, Ilani T, Armony G, Wolf SG, Fass D.
PMID: 32055794
J Struct Biol X. 2019 Jan-Mar;1:100002. doi: 10.1016/j.yjsbx.2018.100002.

Cells and extracellular matrix (ECM) are mutually interdependent: cells guide self-assembly of ECM precursors, and the resulting ECM architecture supports and instructs cells. Though bidirectional signaling between ECM and cells is fundamental to cell biology, it is challenging to...

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Lansky Z, Mutsafi Y, Houben L, et al. 3D mapping of native extracellular matrix reveals cellular responses to the microenvironment. J Struct Biol X. 2019;1:100002doi: 10.1016/j.yjsbx.2018.100002.
Lansky, Z., Mutsafi, Y., Houben, L., Ilani, T., Armony, G., Wolf, S. G., & Fass, D. (2019). 3D mapping of native extracellular matrix reveals cellular responses to the microenvironment. Journal of structural biology: X, 1100002. https://doi.org/10.1016/j.yjsbx.2018.100002
Lansky, Zipora, et al. "3D mapping of native extracellular matrix reveals cellular responses to the microenvironment." Journal of structural biology: X vol. 1 (2019): 100002. doi: https://doi.org/10.1016/j.yjsbx.2018.100002
Lansky Z, Mutsafi Y, Houben L, Ilani T, Armony G, Wolf SG, Fass D. 3D mapping of native extracellular matrix reveals cellular responses to the microenvironment. J Struct Biol X. 2019 Jan-Mar;1:100002. doi: 10.1016/j.yjsbx.2018.100002. PMID: 32055794; PMCID: PMC7001979.
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