Three‐Dimensional Super‐Resolution Imaging of the Midplane Protein FtsZ in Live Caulobacter crescentus Cells Using Astigmatism

Show simple item record Biteen, Julie S. en_US Goley, Erin D. en_US Shapiro, Lucy en_US Moerner, W. E. en_US 2012-04-04T18:43:30Z 2013-05-01T17:24:43Z en_US 2012-03 en_US
dc.identifier.citation Biteen, Julie S.; Goley, Erin D.; Shapiro, Lucy; Moerner, W. E. (2012). "Three‐Dimensional Super‐Resolution Imaging of the Midplane Protein FtsZ in Live Caulobacter crescentus Cells Using Astigmatism." ChemPhysChem 13(4): 1007-1012. <> en_US
dc.identifier.issn 1439-4235 en_US
dc.identifier.issn 1439-7641 en_US
dc.description.abstract Single‐molecule super‐resolution imaging provides a non‐invasive method for nanometer‐scale imaging and is ideally suited to investigations of quasi‐static structures within live cells. Here, we extend the ability to image subcellular features within bacteria cells to three dimensions based on the introduction of a cylindrical lens in the imaging pathway. We investigate the midplane protein FtsZ in Caulobacter crescentus with super‐resolution imaging based on fluorescent‐protein photoswitching and the natural polymerization/depolymerization dynamics of FtsZ associated with the Z‐ring. We quantify these dynamics and determine the FtsZ depolymerization time to be <100 ms. We image the Z‐ring in live and fixed C. crescentus cells at different stages of the cell cycle and find that the FtsZ superstructure is dynamic with the cell cycle, forming an open shape during the stalked stage and a dense focus during the pre‐divisional stage. 3D is here to stay: Three‐dimensional super‐resolution astigmatic optical imaging provides images of the FtsZ Z‐ring in bacterial cells in various stages of the cell cycle. The picture shows, left to right: live stalked cell, live pre‐divisional cell, fixed stalked cell, fixed pre‐divisional cell. Scale bar: 200 nm. en_US
dc.publisher WILEY‐VCH Verlag en_US
dc.subject.other Three‐Dimensional Imaging en_US
dc.subject.other Single‐Molecule Studies en_US
dc.subject.other Proteins en_US
dc.subject.other Live‐Cell Imaging en_US
dc.subject.other Astigmatic Lens en_US
dc.title Three‐Dimensional Super‐Resolution Imaging of the Midplane Protein FtsZ in Live Caulobacter crescentus Cells Using Astigmatism en_US
dc.rights.robots IndexNoFollow en_US
dc.subject.hlbsecondlevel Physics en_US
dc.subject.hlbsecondlevel Chemistry en_US
dc.subject.hlbtoplevel Science en_US
dc.description.peerreviewed Peer Reviewed en_US
dc.contributor.affiliationum Department of Chemistry, University of Michigan, Ann Arbor, MI 48104 (USA) en_US
dc.contributor.affiliationother Department of Chemistry, Stanford University, Stanford, CA 94305 (USA) en_US
dc.contributor.affiliationother Department of Biological Chemistry, Johns Hopkins University, Baltimore, MD 21205 (USA) en_US
dc.contributor.affiliationother Department of Developmental Biology, Stanford University, Stanford, CA 94305 (USA) en_US
dc.contributor.affiliationother Department of Chemistry, Stanford University, Stanford, CA 94305 (USA) en_US
dc.identifier.pmid 22262316 en_US
dc.identifier.doi 10.1002/cphc.201100686 en_US
dc.identifier.source ChemPhysChem en_US
dc.identifier.citedreference N. G. Gurskaya, V. V. Verkhusha, A. S. Shcheglov, D. B. Staroverov, T. V. Chepurnykh, A. F. Fradkov, S. Lukyanov, K. A. Lukyanov, Nat. Biotechnol. 2006, 24, 461 – 465. en_US
dc.identifier.citedreference W. E. Moerner, Nat. Methods 2006, 3, 781 – 782. en_US
dc.identifier.citedreference J. Yu, J. Xiao, X. Ren, K. Lao, X. S. Xie, Science 2006, 311, 1600 – 1603. en_US
dc.identifier.citedreference S. Y. Kim, Z. Gitai, A. Kinkhabwala, L. Shapiro, W. E. Moerner, Proc. Natl. Acad. Sci. USA 2006, 103, 10929 – 10934. en_US
dc.identifier.citedreference E. Betzig, G. H. Patterson, R. Sougrat, O. W. Lindwasser, S. Olenych, J. S. Bonifacino, M. W. Davidson, J. Lippincott‐Schwartz, H. F. Hess, Science 2006, 313, 1642 – 1645. en_US
dc.identifier.citedreference M. J. Rust, M. Bates, X. Zhuang, Nat. Methods 2006, 3, 793 – 796. en_US
dc.identifier.citedreference S. T. Hess, T. P. K. Girirajan, M. D. Mason, Biophys. J. 2006, 91, 4258 – 4272. en_US
dc.identifier.citedreference A. Sharonov, R. M. Hochstrasser, Proc. Natl. Acad. Sci. USA 2006, 103, 18911 – 18916. en_US
dc.identifier.citedreference J. Vogelsang, T. Cordes, C. Forthmann, C. Steinhauer, P. Tinnefeld, Proc. Natl. Acad. Sci. USA 2009, 106, 8107 – 8112. en_US
dc.identifier.citedreference S. F. Lee, M. A. Thompson, M. A. Schwartz, L. Shapiro, W. E. Moerner, Biophys. J. 2011, 100, L31 – L33. en_US
dc.identifier.citedreference G. Fu, T. Huang, J. Buss, C. Coltharp, Z. Hensel, J. Xiao, PLoS One 2010, 5, e 12680. en_US
dc.identifier.citedreference P. C. Jennings, G. C. Cox, L. G. Monahan, E. J. Harry, Micron 2011, 42, 336 – 341. en_US
dc.identifier.citedreference T. A. Planchon, L. Gao, D. E. Milkie, M. W. Davidson, J. A. Galbraith, C. G. Galbraith, E. Betzig, Nat. Methods 2011, 8, 417 – 423. en_US
dc.identifier.citedreference B. Huang, W. Wang, M. Bates, X. Zhuang, Science 2008, 319, 810 – 813. en_US
dc.identifier.citedreference S. A. Jones, S. Shim, J. He, X. Zhuang, Nat. Methods 2011, 8, 499 – 505. en_US
dc.identifier.citedreference M. F. Juette, T. J. Gould, M. D. Lessard, M. J. Mlodzianoski, B. S. Nagpure, B. T. Bennett, S. T. Hess, J. Bewersdorf, Nat. Methods 2008, 5, 527 – 529. en_US
dc.identifier.citedreference J. Fölling, V. Belov, R. Kunetsky, R. Medda, A. Schönle, A. Egner, M. Bossi, S. W. Hell, Angew. Chem. 2007, 119, 6382 – 6386; Angew. Chem. Int. Ed. 2007, 46, 6266 – 6270. en_US
dc.identifier.citedreference G. Shtengel, J. A. Galbraith, C. G. Galbraith, J. Lippincott‐Schwartz, J. M. Gillette, S. Manley, R. Sougrat, C. M. Waterman, P. Kanchanawong, M. W. Davidson, R. D. Fetter, H. F. Hess, Proc. Natl. Acad. Sci. USA 2009, 106, 3125 – 3130. en_US
dc.identifier.citedreference S. R. P. Pavani, M. A. Thompson, J. S. Biteen, S. J. Lord, N. Liu, R. J. Twieg, R. Piestun, W. E. Moerner, Proc. Natl. Acad. Sci. USA 2009, 106, 2995 – 2999. en_US
dc.identifier.citedreference D. E. Anderson, F. J. Guieros‐Filho, H. P. Erickson, J. Bacteriol. 2004, 186, 5775 – 5781. en_US
dc.identifier.citedreference J. Stricker, P. Maddox, E. D. Salmon, H. P. Erickson, Proc. Natl. Acad. Sci. USA 2002, 99, 3171 – 3175. en_US
dc.identifier.citedreference J. S. Biteen, M. A. Thompson, N. K. Tselentis, G. R. Bowman, L. Shapiro, W. E. Moerner, Nat. Methods 2008, 5, 947 – 949. en_US
dc.identifier.citedreference H. P. Kao, A. S. Verkman, Biophys. J. 1994, 67, 1291 – 1300. en_US
dc.identifier.citedreference Y. Deng, J. W. Shaevitz, Appl. Opt. 2009, 48, 1886 – 1890. en_US
dc.identifier.citedreference M. Badieirostami, M. D. Lew, M. A. Thompson, W. E. Moerner, Appl. Phys. Lett. 2010, 97, 161103. en_US
dc.identifier.citedreference R. E. Thompson, D. R. Larson, W. W. Webb, Biophys. J. 2002, 82, 2775 – 2783. en_US
dc.identifier.citedreference J. Engelhardt, J. Keller, P. Hoyer, M. Reuss, T. Staudt, S. W. Hell, Nano Lett. 2011, 11, 209 – 213. en_US
dc.identifier.citedreference W. E. Moerner, D. P. Fromm, Rev. Sci. Instrum. 2003, 74, 3597 – 3619. en_US
dc.identifier.citedreference H. P. Erickson, D. E. Anderson, M. Osawa, Microbiol. Mol. Biol. Rev. 2010, 74, 504 – 528. en_US
dc.identifier.citedreference E. D. Goley, Y. C. Yeh, S. H. Hong, M. J. Fero, E. Abeliuk, H. H. McAdams, L. Shapiro, Mol. Microbiol. 2011, 80, 1680 – 1698. en_US
dc.identifier.citedreference M. Thanbichler, L. Shapiro, Cell 2006, 126, 147 – 162. en_US
dc.identifier.citedreference Z. Li, M. J. Trimble, Y. V. Brun, G. J. Jensen, EMBO J. 2007, 26, 4694 – 4708. en_US
dc.owningcollname Interdisciplinary and Peer-Reviewed
 Show simple item record

This item appears in the following Collection(s)

Search Deep Blue

Advanced Search

Browse by

My Account


Coming Soon

MLibrary logo