Illumination based on objective-type total internal reflection (TIR) is nowadays widely used in high-performance fluorescence microscopy. However, the desirable application of such setups for dark-field imaging of scattering entities is cumbersome due to the spatial overlap of illumination and detection light, which cannot be separated spectrally. Here, we report a novel TIR approach based on a parabolically shaped quartz prism that allows for the detection of single-molecule fluorescence as well as single-particle scattering with high signal-to-noise ratios. We demonstrate homogeneous and spatially invariant illumination profiles in combination with a convenient control over a wide range of illumination angles. Moreover, we quantitatively compare the fluorescence performance of our setup to objective-type TIR and demonstrate sub-nanometer localization accuracies for the scattering of 40 nm gold nanoparticles (AuNPs). When bound to individual kinesin-1 motors, the AuNPs reliably report on the characteristic 8 nm stepping along microtubules.

© 2013 OSA

1. M. Leeuwenhoek and R. de Graaf, “A Specimen of Some Observations Made by a Microscope,” Philos. Trans. Roy. Soc. A.8(92-100), 6037–6038 (1673). [CrossRef]
2. G. Nomarski, “From phase contrast to contrast by interference,” Rev. Hematol. (Paris)12(4), 439–442 (1957). [PubMed]
3. M. Minsky, “Microscopy apparatus,“ U.S. Patent 3,013,467, filed November 7, 1957, and issued December 19, 1961.
4. I. Newton, Opticks (William Innys, London, 1704).
5. D. Axelrod, “Cell-substrate contacts illuminated by total internal reflection fluorescence,” J. Cell Biol.89(1), 141–145 (1981). [CrossRef] [PubMed]
6. D. Axelrod, T. P. Burghardt, and N. L. Thompson, “Total internal reflection fluorescence,” Annu. Rev. Biophys. Bioeng.13(1), 247–268 (1984). [CrossRef] [PubMed]
7. D. Axelrod, “Total internal reflection fluorescence microscopy in cell biology,” Traffic2(11), 764–774 (2001). [CrossRef] [PubMed]
8. R. M. Fulbright and D. Axelrod, “Dynamics of nonspecific adsorption of insulin to erythrocyte membranes,” J. Fluoresc.3(1), 1–16 (1993). [CrossRef]
9. T. Lang, I. Wacker, J. Steyer, C. Kaether, I. Wunderlich, T. Soldati, H. H. Gerdes, and W. Almers, “Ca2+-triggered peptide secretion in single cells imaged with green fluorescent protein and evanescent-wave microscopy,” Neuron18(6), 857–863 (1997). [CrossRef] [PubMed]
10. U. Resch-Genger, M. Grabolle, S. Cavaliere-Jaricot, R. Nitschke, and T. Nann, “Quantum dots versus organic dyes as fluorescent labels,” Nat. Methods5(9), 763–775 (2008). [CrossRef] [PubMed]
11. C. Joo, H. Balci, Y. Ishitsuka, C. Buranachai, and T. Ha, “Advances in single-molecule fluorescence methods for molecular biology,” Annu. Rev. Biochem.77(1), 51–76 (2008). [CrossRef] [PubMed]
12. X. Wang, X. Ren, K. Kahen, M. A. Hahn, M. Rajeswaran, S. Maccagnano-Zacher, J. Silcox, G. E. Cragg, A. L. Efros, and T. D. Krauss, “Non-blinking semiconductor nanocrystals,” Nature459(7247), 686–689 (2009). [CrossRef] [PubMed]
13. M. A. van Dijk, A. L. Tchebotareva, M. Orrit, M. Lippitz, S. Berciaud, D. Lasne, L. Cognet, and B. Lounis, “Absorption and scattering microscopy of single metal nanoparticles,” Phys. Chem. Chem. Phys.8(30), 3486–3495 (2006). [CrossRef] [PubMed]
14. G. Mie, “Beiträge zur Optik trüber Medien, speziell kolloidaler Metallösungen,” Ann. Phys-Berlin330(3), 377–445 (1908). [CrossRef]
15. H. Ueno, S. Nishikawa, R. Iino, K. V. Tabata, S. Sakakihara, T. Yanagida, and H. Noji, “Simple dark-field microscopy with nanometer spatial precision and microsecond temporal resolution,” Biophys. J.98(9), 2014–2023 (2010). [CrossRef] [PubMed]
16. M. van ’t Hoff, M. Reuter, D. T. F. Dryden, and M. Oheim, “Screening by imaging: scaling up single-DNA-molecule analysis with a novel parabolic VA-TIRF reflector and noise-reduction techniques,” Phys. Chem. Chem. Phys.11(35), 7713–7720 (2009). [CrossRef] [PubMed]
17. H. Schneckenburger, “Total internal reflection fluorescence microscopy: technical innovations and novel applications,” Curr. Opin. Biotechnol.16(1), 13–18 (2005). [CrossRef] [PubMed]
18. T. Ruckstuhl, M. Rankl, and S. Seeger, “Confocal TIRF microscopy of single molecules,” P. Soc. Photo-Opt. Ins., Proc. of SPIEE 4962, 126–134 (2003).
19. T. Ruckstuhl and S. Seeger, “Confocal total-internal-reflection fluorescence microscopy with a high-aperture parabolic mirror lens,” Appl. Opt.42(16), 3277–3283 (2003). [CrossRef] [PubMed]
20. H. Välimäki and K. Tappura, “A novel platform for highly surface-sensitive fluorescent measurements applying simultaneous total internal reflection excitation and super critical angle detection,” Chem. Phys. Lett.473(4-6), 358–362 (2009). [CrossRef]
21. C. M. Winterflood, T. Ruckstuhl, D. Verdes, and S. Seeger, “Nanometer axial resolution by three-dimensional supercritical angle fluorescence microscopy,” Phys. Rev. Lett.105(10), 108103 (2010). [CrossRef] [PubMed]
22. E. Lassila, T. Alahautala, and R. Hernberg, “Focusing diode lasers using a truncated paraboloid with spherical output surface,” Opt. Eng.46(5), 054301 (2007). [CrossRef]
23. A. L. Mattheyses, K. Shaw, and D. Axelrod, “Effective elimination of laser interference fringing in fluorescence microscopy by spinning azimuthal incidence angle,” Microsc. Res. Tech.69(8), 642–647 (2006). [CrossRef] [PubMed]
24. R. Fiolka, Y. Belyaev, H. Ewers, and A. Stemmer, “Even illumination in total internal reflection fluorescence microscopy using laser light,” Microsc. Res. Tech.71(1), 45–50 (2008). [CrossRef] [PubMed]
25. C. Gell, M. Berndt, J. Enderlein, and S. Diez, “TIRF microscopy evanescent field calibration using tilted fluorescent microtubules,” J. Microsc.234(1), 38–46 (2009). [CrossRef] [PubMed]
26. W. P. Ambrose, P. M. Goodwin, and J. P. Nolan, “Single-molecule detection with total internal reflection excitation: Comparing signal-to-background and total signals in different geometries,” Cytometry36(3), 224–231 (1999). [CrossRef] [PubMed]
27. S. Verbrugge, S. M. J. L. van den Wildenberg, and E. J. G. Peterman, “Novel ways to determine kinesin-1’s run length and randomness using fluorescence microscopy,” Biophys. J.97(8), 2287–2294 (2009). [CrossRef] [PubMed]
28. G. I. Mashanov, D. Tacon, M. Peckham, and J. E. Molloy, “The spatial and temporal dynamics of pleckstrin homology domain binding at the plasma membrane measured by imaging single molecules in live mouse myoblasts,” J. Biol. Chem.279(15), 15274–15280 (2004). [CrossRef] [PubMed]
29. T. Ruckstuhl, J. Enderlein, S. Jung, and S. Seeger, “Forbidden Light Detection from Single Molecules,” Anal. Chem.72(9), 2117–2123 (2000). [CrossRef] [PubMed]
30. J. Enderlein and T. Ruckstuhl, “The efficiency of surface-plasmon coupled emission for sensitive fluorescence detection,” Opt. Express13(22), 8855–8865 (2005). [CrossRef] [PubMed]
31. A. Yildiz, M. Tomishige, R. D. Vale, and P. R. Selvin, “Kinesin walks hand-over-hand,” Science303(5658), 676–678 (2004). [CrossRef] [PubMed]
32. A. R. Dunn and J. A. Spudich, “Dynamics of the unbound head during myosin V processive translocation,” Nat. Struct. Mol. Biol.14(3), 246–248 (2007). [CrossRef] [PubMed]
33. R. E. Thompson, D. R. Larson, and W. W. Webb, “Precise nanometer localization analysis for individual fluorescent probes,” Biophys. J.82(5), 2775–2783 (2002). [CrossRef] [PubMed]
34. R. Swaminathan, C. P. Hoang, and A. S. Verkman, “Photobleaching recovery and anisotropy decay of green fluorescent protein GFP-S65T in solution and cells: Cytoplasmic viscosity probed by green fluorescent protein translational and rotational diffusion,” Biophys. J.72(4), 1900–1907 (1997). [CrossRef] [PubMed]
35. F. Ruhnow, D. Zwicker, and S. Diez, “Tracking single particles and elongated filaments with nanometer precision,” Biophys. J.100(11), 2820–2828 (2011). [CrossRef] [PubMed]
36. J. W. J. Kerssemakers, E. L. Munteanu, L. Laan, T. L. Noetzel, M. E. Janson, and M. Dogterom, “Assembly dynamics of microtubules at molecular resolution,” Nature442(7103), 709–712 (2006). [CrossRef] [PubMed]
37. M. J. Schnitzer and S. M. Block, “Kinesin hydrolyses one ATP per 8-nm step,” Nature388(6640), 386–390 (1997). [CrossRef] [PubMed]
38. C. Gell, V. Bormuth, G. J. Brouhard, D. N. Cohen, S. Diez, C. T. Friel, J. Helenius, B. Nitzsche, H. Petzold, J. Ribbe, E. Schäffer, J. H. Stear, A. Trushko, V. Varga, P. O. Widlund, M. Zanic, and J. Howard, “Microtubule dynamics reconstituted in vitro and imaged by single-molecule fluorescence microscopy,” Methods Cell Biol.95, 221–245 (2010). [CrossRef] [PubMed]
39. K. R. Rogers, S. Weiss, I. Crevel, P. J. Brophy, M. Geeves, and R. Cross, “KIF1D is a fast non-processive kinesin that demonstrates novel K-loop-dependent mechanochemistry,” EMBO J.20(18), 5101–5113 (2001). [CrossRef] [PubMed]
40. W. Haiss, N. T. K. Thanh, J. Aveyard, and D. G. Fernig, “Determination of Size and Concentration of Gold Nanoparticles from UV-Vis Spectra,” Anal. Chem.79(11), 4215–4221 (2007). [CrossRef] [PubMed]

Alahautala, T.
Almers, W.
Ambrose, W. P.
Aveyard, J.
Axelrod, D.
Balci, H.
Belyaev, Y.
Berciaud, S.
Berndt, M.
Block, S. M.
Bormuth, V.
Brophy, P. J.
Brouhard, G. J.
Buranachai, C.
Burghardt, T. P.
Cavaliere-Jaricot, S.
Cognet, L.
Cohen, D. N.
Cragg, G. E.
Crevel, I.
Cross, R.
de Graaf, R.
Diez, S.
Dogterom, M.
Dryden, D. T. F.
Dunn, A. R.
Efros, A. L.
Enderlein, J.
Ewers, H.
Fernig, D. G.
Fiolka, R.
Friel, C. T.
Fulbright, R. M.
Geeves, M.
Gell, C.
Gerdes, H. H.
Goodwin, P. M.
Grabolle, M.
Ha, T.
Hahn, M. A.
Haiss, W.
Helenius, J.
Hernberg, R.
Hoang, C. P.
Howard, J.
Iino, R.
Ishitsuka, Y.
Janson, M. E.
Joo, C.
Jung, S.
Kaether, C.
Kahen, K.
Kerssemakers, J. W. J.
Krauss, T. D.
Laan, L.
Lang, T.
Larson, D. R.
Lasne, D.
Lassila, E.
Leeuwenhoek, M.
Lippitz, M.
Lounis, B.
Maccagnano-Zacher, S.
Mashanov, G. I.
Mattheyses, A. L.
Mie, G.
Molloy, J. E.
Munteanu, E. L.
Nann, T.
Nishikawa, S.
Nitschke, R.
Nitzsche, B.
Noetzel, T. L.
Noji, H.
Nolan, J. P.
Nomarski, G.
Oheim, M.
Orrit, M.
Peckham, M.
Peterman, E. J. G.
Petzold, H.
Rajeswaran, M.
Ren, X.
Resch-Genger, U.
Reuter, M.
Ribbe, J.
Rogers, K. R.
Ruckstuhl, T.
Ruhnow, F.
Sakakihara, S.
Schäffer, E.
Schneckenburger, H.
Schnitzer, M. J.
Seeger, S.
Selvin, P. R.
Shaw, K.
Silcox, J.
Soldati, T.
Spudich, J. A.
Stear, J. H.
Stemmer, A.
Steyer, J.
Swaminathan, R.
Tabata, K. V.
Tacon, D.
Tappura, K.
Tchebotareva, A. L.
Thanh, N. T. K.
Thompson, N. L.
Thompson, R. E.
Tomishige, M.
Trushko, A.
Ueno, H.
Vale, R. D.
Välimäki, H.
van ’t Hoff, M.
van den Wildenberg, S. M. J. L.
van Dijk, M. A.
Varga, V.
Verbrugge, S.
Verdes, D.
Verkman, A. S.
Wacker, I.
Wang, X.
Webb, W. W.
Weiss, S.
Widlund, P. O.
Winterflood, C. M.
Wunderlich, I.
Yanagida, T.
Yildiz, A.
Zanic, M.
Zwicker, D.

Anal. Chem.

• T. Ruckstuhl, J. Enderlein, S. Jung, and S. Seeger, “Forbidden Light Detection from Single Molecules,” Anal. Chem.72(9), 2117–2123 (2000). [CrossRef] [PubMed]
• W. Haiss, N. T. K. Thanh, J. Aveyard, and D. G. Fernig, “Determination of Size and Concentration of Gold Nanoparticles from UV-Vis Spectra,” Anal. Chem.79(11), 4215–4221 (2007). [CrossRef] [PubMed]

Ann. Phys-Berlin

• G. Mie, “Beiträge zur Optik trüber Medien, speziell kolloidaler Metallösungen,” Ann. Phys-Berlin330(3), 377–445 (1908). [CrossRef]

Annu. Rev. Biochem.

• C. Joo, H. Balci, Y. Ishitsuka, C. Buranachai, and T. Ha, “Advances in single-molecule fluorescence methods for molecular biology,” Annu. Rev. Biochem.77(1), 51–76 (2008). [CrossRef] [PubMed]

Annu. Rev. Biophys. Bioeng.

• D. Axelrod, T. P. Burghardt, and N. L. Thompson, “Total internal reflection fluorescence,” Annu. Rev. Biophys. Bioeng.13(1), 247–268 (1984). [CrossRef] [PubMed]

Appl. Opt.

• T. Ruckstuhl and S. Seeger, “Confocal total-internal-reflection fluorescence microscopy with a high-aperture parabolic mirror lens,” Appl. Opt.42(16), 3277–3283 (2003). [CrossRef] [PubMed]

Biophys. J.

• S. Verbrugge, S. M. J. L. van den Wildenberg, and E. J. G. Peterman, “Novel ways to determine kinesin-1’s run length and randomness using fluorescence microscopy,” Biophys. J.97(8), 2287–2294 (2009). [CrossRef] [PubMed]
• R. E. Thompson, D. R. Larson, and W. W. Webb, “Precise nanometer localization analysis for individual fluorescent probes,” Biophys. J.82(5), 2775–2783 (2002). [CrossRef] [PubMed]
• R. Swaminathan, C. P. Hoang, and A. S. Verkman, “Photobleaching recovery and anisotropy decay of green fluorescent protein GFP-S65T in solution and cells: Cytoplasmic viscosity probed by green fluorescent protein translational and rotational diffusion,” Biophys. J.72(4), 1900–1907 (1997). [CrossRef] [PubMed]
• F. Ruhnow, D. Zwicker, and S. Diez, “Tracking single particles and elongated filaments with nanometer precision,” Biophys. J.100(11), 2820–2828 (2011). [CrossRef] [PubMed]
• H. Ueno, S. Nishikawa, R. Iino, K. V. Tabata, S. Sakakihara, T. Yanagida, and H. Noji, “Simple dark-field microscopy with nanometer spatial precision and microsecond temporal resolution,” Biophys. J.98(9), 2014–2023 (2010). [CrossRef] [PubMed]

Chem. Phys. Lett.

• H. Välimäki and K. Tappura, “A novel platform for highly surface-sensitive fluorescent measurements applying simultaneous total internal reflection excitation and super critical angle detection,” Chem. Phys. Lett.473(4-6), 358–362 (2009). [CrossRef]

Curr. Opin. Biotechnol.

• H. Schneckenburger, “Total internal reflection fluorescence microscopy: technical innovations and novel applications,” Curr. Opin. Biotechnol.16(1), 13–18 (2005). [CrossRef] [PubMed]

Cytometry

• W. P. Ambrose, P. M. Goodwin, and J. P. Nolan, “Single-molecule detection with total internal reflection excitation: Comparing signal-to-background and total signals in different geometries,” Cytometry36(3), 224–231 (1999). [CrossRef] [PubMed]

EMBO J.

• K. R. Rogers, S. Weiss, I. Crevel, P. J. Brophy, M. Geeves, and R. Cross, “KIF1D is a fast non-processive kinesin that demonstrates novel K-loop-dependent mechanochemistry,” EMBO J.20(18), 5101–5113 (2001). [CrossRef] [PubMed]

J. Biol. Chem.

• G. I. Mashanov, D. Tacon, M. Peckham, and J. E. Molloy, “The spatial and temporal dynamics of pleckstrin homology domain binding at the plasma membrane measured by imaging single molecules in live mouse myoblasts,” J. Biol. Chem.279(15), 15274–15280 (2004). [CrossRef] [PubMed]

J. Cell Biol.

• D. Axelrod, “Cell-substrate contacts illuminated by total internal reflection fluorescence,” J. Cell Biol.89(1), 141–145 (1981). [CrossRef] [PubMed]

J. Fluoresc.

• R. M. Fulbright and D. Axelrod, “Dynamics of nonspecific adsorption of insulin to erythrocyte membranes,” J. Fluoresc.3(1), 1–16 (1993). [CrossRef]

J. Microsc.

• C. Gell, M. Berndt, J. Enderlein, and S. Diez, “TIRF microscopy evanescent field calibration using tilted fluorescent microtubules,” J. Microsc.234(1), 38–46 (2009). [CrossRef] [PubMed]

Methods Cell Biol.

• C. Gell, V. Bormuth, G. J. Brouhard, D. N. Cohen, S. Diez, C. T. Friel, J. Helenius, B. Nitzsche, H. Petzold, J. Ribbe, E. Schäffer, J. H. Stear, A. Trushko, V. Varga, P. O. Widlund, M. Zanic, and J. Howard, “Microtubule dynamics reconstituted in vitro and imaged by single-molecule fluorescence microscopy,” Methods Cell Biol.95, 221–245 (2010). [CrossRef] [PubMed]

Microsc. Res. Tech.

• A. L. Mattheyses, K. Shaw, and D. Axelrod, “Effective elimination of laser interference fringing in fluorescence microscopy by spinning azimuthal incidence angle,” Microsc. Res. Tech.69(8), 642–647 (2006). [CrossRef] [PubMed]
• R. Fiolka, Y. Belyaev, H. Ewers, and A. Stemmer, “Even illumination in total internal reflection fluorescence microscopy using laser light,” Microsc. Res. Tech.71(1), 45–50 (2008). [CrossRef] [PubMed]

Nat. Methods

• U. Resch-Genger, M. Grabolle, S. Cavaliere-Jaricot, R. Nitschke, and T. Nann, “Quantum dots versus organic dyes as fluorescent labels,” Nat. Methods5(9), 763–775 (2008). [CrossRef] [PubMed]

Nat. Struct. Mol. Biol.

• A. R. Dunn and J. A. Spudich, “Dynamics of the unbound head during myosin V processive translocation,” Nat. Struct. Mol. Biol.14(3), 246–248 (2007). [CrossRef] [PubMed]

Nature

• J. W. J. Kerssemakers, E. L. Munteanu, L. Laan, T. L. Noetzel, M. E. Janson, and M. Dogterom, “Assembly dynamics of microtubules at molecular resolution,” Nature442(7103), 709–712 (2006). [CrossRef] [PubMed]
• M. J. Schnitzer and S. M. Block, “Kinesin hydrolyses one ATP per 8-nm step,” Nature388(6640), 386–390 (1997). [CrossRef] [PubMed]
• X. Wang, X. Ren, K. Kahen, M. A. Hahn, M. Rajeswaran, S. Maccagnano-Zacher, J. Silcox, G. E. Cragg, A. L. Efros, and T. D. Krauss, “Non-blinking semiconductor nanocrystals,” Nature459(7247), 686–689 (2009). [CrossRef] [PubMed]

Neuron

• T. Lang, I. Wacker, J. Steyer, C. Kaether, I. Wunderlich, T. Soldati, H. H. Gerdes, and W. Almers, “Ca2+-triggered peptide secretion in single cells imaged with green fluorescent protein and evanescent-wave microscopy,” Neuron18(6), 857–863 (1997). [CrossRef] [PubMed]

Opt. Eng.

• E. Lassila, T. Alahautala, and R. Hernberg, “Focusing diode lasers using a truncated paraboloid with spherical output surface,” Opt. Eng.46(5), 054301 (2007). [CrossRef]

Opt. Express

• J. Enderlein and T. Ruckstuhl, “The efficiency of surface-plasmon coupled emission for sensitive fluorescence detection,” Opt. Express13(22), 8855–8865 (2005). [CrossRef] [PubMed]

Philos. Trans. Roy. Soc. A.

• M. Leeuwenhoek and R. de Graaf, “A Specimen of Some Observations Made by a Microscope,” Philos. Trans. Roy. Soc. A.8(92-100), 6037–6038 (1673). [CrossRef]

Phys. Chem. Chem. Phys.

• M. A. van Dijk, A. L. Tchebotareva, M. Orrit, M. Lippitz, S. Berciaud, D. Lasne, L. Cognet, and B. Lounis, “Absorption and scattering microscopy of single metal nanoparticles,” Phys. Chem. Chem. Phys.8(30), 3486–3495 (2006). [CrossRef] [PubMed]
• M. van ’t Hoff, M. Reuter, D. T. F. Dryden, and M. Oheim, “Screening by imaging: scaling up single-DNA-molecule analysis with a novel parabolic VA-TIRF reflector and noise-reduction techniques,” Phys. Chem. Chem. Phys.11(35), 7713–7720 (2009). [CrossRef] [PubMed]

Phys. Rev. Lett.

• C. M. Winterflood, T. Ruckstuhl, D. Verdes, and S. Seeger, “Nanometer axial resolution by three-dimensional supercritical angle fluorescence microscopy,” Phys. Rev. Lett.105(10), 108103 (2010). [CrossRef] [PubMed]

Rev. Hematol. (Paris)

• G. Nomarski, “From phase contrast to contrast by interference,” Rev. Hematol. (Paris)12(4), 439–442 (1957). [PubMed]

Science

• A. Yildiz, M. Tomishige, R. D. Vale, and P. R. Selvin, “Kinesin walks hand-over-hand,” Science303(5658), 676–678 (2004). [CrossRef] [PubMed]

Traffic

• D. Axelrod, “Total internal reflection fluorescence microscopy in cell biology,” Traffic2(11), 764–774 (2001). [CrossRef] [PubMed]

Other

• M. Minsky, “Microscopy apparatus,“ U.S. Patent 3,013,467, filed November 7, 1957, and issued December 19, 1961.
• I. Newton, Opticks (William Innys, London, 1704).
• T. Ruckstuhl, M. Rankl, and S. Seeger, “Confocal TIRF microscopy of single molecules,” P. Soc. Photo-Opt. Ins., Proc. of SPIEE 4962, 126–134 (2003).

2011, Ruhnow, Biophys. J.
2010, Gell, Methods Cell Biol.
2010, Winterflood, Phys. Rev. Lett.
2010, Ueno, Biophys. J.
2009, van ’t Hoff, Phys. Chem. Chem. Phys.
2009, Wang, Nature
2009, Välimäki, Chem. Phys. Lett.
2009, Gell, J. Microsc.
2009, Verbrugge, Biophys. J.
2008, Fiolka, Microsc. Res. Tech.
2008, Resch-Genger, Nat. Methods
2008, Joo, Annu. Rev. Biochem.
2007, Haiss, Anal. Chem.
2007, Dunn, Nat. Struct. Mol. Biol.
2007, Lassila, Opt. Eng.
2006, Mattheyses, Microsc. Res. Tech.
2006, Kerssemakers, Nature
2006, van Dijk, Phys. Chem. Chem. Phys.
2005, Schneckenburger, Curr. Opin. Biotechnol.
2005, Enderlein, Opt. Express
2004, Yildiz, Science
2004, Mashanov, J. Biol. Chem.
2003, Ruckstuhl, Appl. Opt.
2002, Thompson, Biophys. J.
2001, Rogers, EMBO J.
2001, Axelrod, Traffic
2000, Ruckstuhl, Anal. Chem.
1999, Ambrose, Cytometry
1997, Swaminathan, Biophys. J.
1997, Schnitzer, Nature
1997, Lang, Neuron
1993, Fulbright, J. Fluoresc.
1984, Axelrod, Annu. Rev. Biophys. Bioeng.
1981, Axelrod, J. Cell Biol.
1957, Nomarski, Rev. Hematol. (Paris)
1908, Mie, Ann. Phys-Berlin
1673, Leeuwenhoek, Philos. Trans. Roy. Soc. A.

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