Abstract

In atomic force microscopy (AFM), finding sparsely distributed regions of interest can be difficult and time-consuming. Typically, the tip is scanned until the desired object is located. This process can mechanically or chemically degrade the tip, as well as damage fragile biological samples. Protein assemblies can be detected using the back-scattered light from a focused laser beam. We previously used back-scattered light from a pair of laser foci to stabilize an AFM. In the present work, we integrate these techniques to optically image patches of purple membranes prior to AFM investigation. These rapidly acquired optical images were aligned to the subsequent AFM images to ~40 nm, since the tip position was aligned to the optical axis of the imaging laser. Thus, this label-free imaging efficiently locates sparsely distributed protein assemblies for subsequent AFM study while simultaneously minimizing degradation of the tip and the sample.

© 2010 OSA

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    [CrossRef] [PubMed]
  2. M. Rief, M. Gautel, F. Oesterhelt, J. M. Fernandez, and H. E. Gaub, “Reversible unfolding of individual titin immunoglobulin domains by AFM,” Science 276(5315), 1109–1112 (1997).
    [CrossRef] [PubMed]
  3. S. Scheuring and J. N. Sturgis, “Chromatic adaptation of photosynthetic membranes,” Science 309(5733), 484–487 (2005).
    [CrossRef] [PubMed]
  4. C. D. Frisbie, L. F. Rozsnyai, A. Noy, M. S. Wrighton, and C. M. Lieber, “Functional group imaging by chemical force microscopy,” Science 265(5181), 2071–2074 (1994).
    [CrossRef] [PubMed]
  5. F. Oesterhelt, D. Oesterhelt, M. Pfeiffer, A. Engel, H. E. Gaub, and D. J. Müller, “Unfolding pathways of individual bacteriorhodopsins,” Science 288(5463), 143–146 (2000).
    [CrossRef] [PubMed]
  6. S. M. Block, K. A. Fahrner, and H. C. Berg, “Visualization of bacterial flagella by video-enhanced light microscopy,” J. Bacteriol. 173(2), 933–936 (1991).
    [PubMed]
  7. R. A. Lugmaier, T. Hugel, M. Benoit, and H. E. Gaub, “Phase contrast and DIC illumination for AFM hybrids,” Ultramicroscopy 104(3-4), 255–260 (2005).
    [CrossRef] [PubMed]
  8. A. Yildiz, J. N. Forkey, S. A. McKinney, T. Ha, Y. E. Goldman, and P. R. Selvin, “Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization,” Science 300(5628), 2061–2065 (2003).
    [CrossRef] [PubMed]
  9. H. Yamada, H. Tokumoto, S. Akamine, K. Fukuzawa, and H. Kuwano, “Imaging of organic molecular films using a scanning near-field optical microscope combined with an atomic force microscope,” J. Vac. Sci. Technol. B 14(2), 812–815 (1996).
    [CrossRef]
  10. C. A. J. Putman, H. G. Hansma, H. E. Gaub, and P. K. Hansma, “Polymerized Lb Films Imaged with a Combined Atomic Force Microscope Fluorescence Microscope,” Langmuir 8(12), 3014–3019 (1992).
    [CrossRef]
  11. A. B. Mathur, G. A. Truskey, and W. M. Reichert, “Atomic force and total internal reflection fluorescence microscopy for the study of force transmission in endothelial cells,” Biophys. J. 78(4), 1725–1735 (2000).
    [CrossRef] [PubMed]
  12. H. Gumpp, S. W. Stahl, M. Strackharn, E. M. Puchner, and H. E. Gaub, “Ultrastable combined atomic force and total internal reflection fluorescence microscope [corrected],” Rev. Sci. Instrum. 80(6), 063704 (2009).
    [CrossRef] [PubMed]
  13. H. Ewers, V. Jacobsen, E. Klotzsch, A. E. Smith, A. Helenius, and V. Sandoghdar, “Label-free optical detection and tracking of single virions bound to their receptors in supported membrane bilayers,” Nano Lett. 7(8), 2263–2266 (2007).
    [CrossRef] [PubMed]
  14. V. Jacobsen, P. Stoller, C. Brunner, V. Vogel, and V. Sandoghdar, “Interferometric optical detection and tracking of very small gold nanoparticles at a water-glass interface,” Opt. Express 14(1), 405–414 (2006).
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    [CrossRef] [PubMed]
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    [CrossRef] [PubMed]
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    [CrossRef]
  19. R. P. Gonçalves, G. Agnus, P. Sens, C. Houssin, B. Bartenlian, and S. Scheuring, “Two-chamber AFM: probing membrane proteins separating two aqueous compartments,” Nat. Methods 3(12), 1007–1012 (2006).
    [CrossRef] [PubMed]
  20. D. J. Müller and A. Engel, “Atomic force microscopy and spectroscopy of native membrane proteins,” Nat. Protoc. 2(9), 2191–2197 (2007).
    [CrossRef] [PubMed]
  21. Y. Shichida, S. Matuoka, Y. Hidaka, and T. Yoshizawa, “Absorption spectra of intermediate of bacteriorhodopsin measured by laser photolysis at room temperatures,” Biochim. Biophys. Acta 723(2), 240–246 (1983).
    [CrossRef]
  22. D. J. Müller and A. Engel, “The height of biomolecules measured with the atomic force microscope depends on electrostatic interactions,” Biophys. J. 73(3), 1633–1644 (1997).
    [CrossRef] [PubMed]
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  24. A. Lukács, G. Garab, and E. Papp, “Measurement of the optical parameters of purple membrane and plant light-harvesting complex films with optical waveguide lightmode spectroscopy,” Biosens. Bioelectron. 21(8), 1606–1612 (2006).
    [CrossRef] [PubMed]
  25. H. Michel and D. Oesterhelt, “Three-dimensional crystals of membrane proteins: bacteriorhodopsin,” Proc. Natl. Acad. Sci. U.S.A. 77(3), 1283–1285 (1980).
    [CrossRef] [PubMed]

2009 (2)

H. Gumpp, S. W. Stahl, M. Strackharn, E. M. Puchner, and H. E. Gaub, “Ultrastable combined atomic force and total internal reflection fluorescence microscope [corrected],” Rev. Sci. Instrum. 80(6), 063704 (2009).
[CrossRef] [PubMed]

G. M. King, A. R. Carter, A. B. Churnside, L. S. Eberle, and T. T. Perkins, “Ultrastable atomic force microscopy: atomic-scale lateral stability and registration in ambient condition,” Nano Lett. 9(4), 1451–1456 (2009).
[CrossRef] [PubMed]

2007 (4)

A. R. Carter, G. M. King, T. A. Ulrich, W. Halsey, D. Alchenberger, and T. T. Perkins, “Stabilization of an optical microscope to 0.1 nm in three dimensions,” Appl. Opt. 46(3), 421–427 (2007).
[CrossRef] [PubMed]

A. R. Carter, G. M. King, and T. T. Perkins, “Back-scattered detection provides atomic-scale localization precision, stability, and registration in 3D,” Opt. Express 15(20), 13434–13445 (2007).
[CrossRef] [PubMed]

H. Ewers, V. Jacobsen, E. Klotzsch, A. E. Smith, A. Helenius, and V. Sandoghdar, “Label-free optical detection and tracking of single virions bound to their receptors in supported membrane bilayers,” Nano Lett. 7(8), 2263–2266 (2007).
[CrossRef] [PubMed]

D. J. Müller and A. Engel, “Atomic force microscopy and spectroscopy of native membrane proteins,” Nat. Protoc. 2(9), 2191–2197 (2007).
[CrossRef] [PubMed]

2006 (3)

R. P. Gonçalves, G. Agnus, P. Sens, C. Houssin, B. Bartenlian, and S. Scheuring, “Two-chamber AFM: probing membrane proteins separating two aqueous compartments,” Nat. Methods 3(12), 1007–1012 (2006).
[CrossRef] [PubMed]

V. Jacobsen, P. Stoller, C. Brunner, V. Vogel, and V. Sandoghdar, “Interferometric optical detection and tracking of very small gold nanoparticles at a water-glass interface,” Opt. Express 14(1), 405–414 (2006).
[CrossRef] [PubMed]

A. Lukács, G. Garab, and E. Papp, “Measurement of the optical parameters of purple membrane and plant light-harvesting complex films with optical waveguide lightmode spectroscopy,” Biosens. Bioelectron. 21(8), 1606–1612 (2006).
[CrossRef] [PubMed]

2005 (2)

S. Scheuring and J. N. Sturgis, “Chromatic adaptation of photosynthetic membranes,” Science 309(5733), 484–487 (2005).
[CrossRef] [PubMed]

R. A. Lugmaier, T. Hugel, M. Benoit, and H. E. Gaub, “Phase contrast and DIC illumination for AFM hybrids,” Ultramicroscopy 104(3-4), 255–260 (2005).
[CrossRef] [PubMed]

2003 (1)

A. Yildiz, J. N. Forkey, S. A. McKinney, T. Ha, Y. E. Goldman, and P. R. Selvin, “Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization,” Science 300(5628), 2061–2065 (2003).
[CrossRef] [PubMed]

2000 (2)

A. B. Mathur, G. A. Truskey, and W. M. Reichert, “Atomic force and total internal reflection fluorescence microscopy for the study of force transmission in endothelial cells,” Biophys. J. 78(4), 1725–1735 (2000).
[CrossRef] [PubMed]

F. Oesterhelt, D. Oesterhelt, M. Pfeiffer, A. Engel, H. E. Gaub, and D. J. Müller, “Unfolding pathways of individual bacteriorhodopsins,” Science 288(5463), 143–146 (2000).
[CrossRef] [PubMed]

1997 (2)

M. Rief, M. Gautel, F. Oesterhelt, J. M. Fernandez, and H. E. Gaub, “Reversible unfolding of individual titin immunoglobulin domains by AFM,” Science 276(5315), 1109–1112 (1997).
[CrossRef] [PubMed]

D. J. Müller and A. Engel, “The height of biomolecules measured with the atomic force microscope depends on electrostatic interactions,” Biophys. J. 73(3), 1633–1644 (1997).
[CrossRef] [PubMed]

1996 (1)

H. Yamada, H. Tokumoto, S. Akamine, K. Fukuzawa, and H. Kuwano, “Imaging of organic molecular films using a scanning near-field optical microscope combined with an atomic force microscope,” J. Vac. Sci. Technol. B 14(2), 812–815 (1996).
[CrossRef]

1994 (1)

C. D. Frisbie, L. F. Rozsnyai, A. Noy, M. S. Wrighton, and C. M. Lieber, “Functional group imaging by chemical force microscopy,” Science 265(5181), 2071–2074 (1994).
[CrossRef] [PubMed]

1992 (1)

C. A. J. Putman, H. G. Hansma, H. E. Gaub, and P. K. Hansma, “Polymerized Lb Films Imaged with a Combined Atomic Force Microscope Fluorescence Microscope,” Langmuir 8(12), 3014–3019 (1992).
[CrossRef]

1991 (1)

S. M. Block, K. A. Fahrner, and H. C. Berg, “Visualization of bacterial flagella by video-enhanced light microscopy,” J. Bacteriol. 173(2), 933–936 (1991).
[PubMed]

1988 (1)

G. Meyer and N. M. Amer, “Novel Optical Approach to Atomic Force Microscopy,” Appl. Phys. Lett. 53(12), 1045–1047 (1988).
[CrossRef]

1986 (1)

G. Binnig, C. F. Quate, and C. Gerber, “Atomic force microscope,” Phys. Rev. Lett. 56(9), 930–933 (1986).
[CrossRef] [PubMed]

1983 (1)

Y. Shichida, S. Matuoka, Y. Hidaka, and T. Yoshizawa, “Absorption spectra of intermediate of bacteriorhodopsin measured by laser photolysis at room temperatures,” Biochim. Biophys. Acta 723(2), 240–246 (1983).
[CrossRef]

1980 (1)

H. Michel and D. Oesterhelt, “Three-dimensional crystals of membrane proteins: bacteriorhodopsin,” Proc. Natl. Acad. Sci. U.S.A. 77(3), 1283–1285 (1980).
[CrossRef] [PubMed]

Agnus, G.

R. P. Gonçalves, G. Agnus, P. Sens, C. Houssin, B. Bartenlian, and S. Scheuring, “Two-chamber AFM: probing membrane proteins separating two aqueous compartments,” Nat. Methods 3(12), 1007–1012 (2006).
[CrossRef] [PubMed]

Akamine, S.

H. Yamada, H. Tokumoto, S. Akamine, K. Fukuzawa, and H. Kuwano, “Imaging of organic molecular films using a scanning near-field optical microscope combined with an atomic force microscope,” J. Vac. Sci. Technol. B 14(2), 812–815 (1996).
[CrossRef]

Alchenberger, D.

Amer, N. M.

G. Meyer and N. M. Amer, “Novel Optical Approach to Atomic Force Microscopy,” Appl. Phys. Lett. 53(12), 1045–1047 (1988).
[CrossRef]

Bartenlian, B.

R. P. Gonçalves, G. Agnus, P. Sens, C. Houssin, B. Bartenlian, and S. Scheuring, “Two-chamber AFM: probing membrane proteins separating two aqueous compartments,” Nat. Methods 3(12), 1007–1012 (2006).
[CrossRef] [PubMed]

Benoit, M.

R. A. Lugmaier, T. Hugel, M. Benoit, and H. E. Gaub, “Phase contrast and DIC illumination for AFM hybrids,” Ultramicroscopy 104(3-4), 255–260 (2005).
[CrossRef] [PubMed]

Berg, H. C.

S. M. Block, K. A. Fahrner, and H. C. Berg, “Visualization of bacterial flagella by video-enhanced light microscopy,” J. Bacteriol. 173(2), 933–936 (1991).
[PubMed]

Binnig, G.

G. Binnig, C. F. Quate, and C. Gerber, “Atomic force microscope,” Phys. Rev. Lett. 56(9), 930–933 (1986).
[CrossRef] [PubMed]

Block, S. M.

S. M. Block, K. A. Fahrner, and H. C. Berg, “Visualization of bacterial flagella by video-enhanced light microscopy,” J. Bacteriol. 173(2), 933–936 (1991).
[PubMed]

Brunner, C.

Carter, A. R.

Churnside, A. B.

G. M. King, A. R. Carter, A. B. Churnside, L. S. Eberle, and T. T. Perkins, “Ultrastable atomic force microscopy: atomic-scale lateral stability and registration in ambient condition,” Nano Lett. 9(4), 1451–1456 (2009).
[CrossRef] [PubMed]

Eberle, L. S.

G. M. King, A. R. Carter, A. B. Churnside, L. S. Eberle, and T. T. Perkins, “Ultrastable atomic force microscopy: atomic-scale lateral stability and registration in ambient condition,” Nano Lett. 9(4), 1451–1456 (2009).
[CrossRef] [PubMed]

Engel, A.

D. J. Müller and A. Engel, “Atomic force microscopy and spectroscopy of native membrane proteins,” Nat. Protoc. 2(9), 2191–2197 (2007).
[CrossRef] [PubMed]

F. Oesterhelt, D. Oesterhelt, M. Pfeiffer, A. Engel, H. E. Gaub, and D. J. Müller, “Unfolding pathways of individual bacteriorhodopsins,” Science 288(5463), 143–146 (2000).
[CrossRef] [PubMed]

D. J. Müller and A. Engel, “The height of biomolecules measured with the atomic force microscope depends on electrostatic interactions,” Biophys. J. 73(3), 1633–1644 (1997).
[CrossRef] [PubMed]

Ewers, H.

H. Ewers, V. Jacobsen, E. Klotzsch, A. E. Smith, A. Helenius, and V. Sandoghdar, “Label-free optical detection and tracking of single virions bound to their receptors in supported membrane bilayers,” Nano Lett. 7(8), 2263–2266 (2007).
[CrossRef] [PubMed]

Fahrner, K. A.

S. M. Block, K. A. Fahrner, and H. C. Berg, “Visualization of bacterial flagella by video-enhanced light microscopy,” J. Bacteriol. 173(2), 933–936 (1991).
[PubMed]

Fernandez, J. M.

M. Rief, M. Gautel, F. Oesterhelt, J. M. Fernandez, and H. E. Gaub, “Reversible unfolding of individual titin immunoglobulin domains by AFM,” Science 276(5315), 1109–1112 (1997).
[CrossRef] [PubMed]

Forkey, J. N.

A. Yildiz, J. N. Forkey, S. A. McKinney, T. Ha, Y. E. Goldman, and P. R. Selvin, “Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization,” Science 300(5628), 2061–2065 (2003).
[CrossRef] [PubMed]

Frisbie, C. D.

C. D. Frisbie, L. F. Rozsnyai, A. Noy, M. S. Wrighton, and C. M. Lieber, “Functional group imaging by chemical force microscopy,” Science 265(5181), 2071–2074 (1994).
[CrossRef] [PubMed]

Fukuzawa, K.

H. Yamada, H. Tokumoto, S. Akamine, K. Fukuzawa, and H. Kuwano, “Imaging of organic molecular films using a scanning near-field optical microscope combined with an atomic force microscope,” J. Vac. Sci. Technol. B 14(2), 812–815 (1996).
[CrossRef]

Garab, G.

A. Lukács, G. Garab, and E. Papp, “Measurement of the optical parameters of purple membrane and plant light-harvesting complex films with optical waveguide lightmode spectroscopy,” Biosens. Bioelectron. 21(8), 1606–1612 (2006).
[CrossRef] [PubMed]

Gaub, H. E.

H. Gumpp, S. W. Stahl, M. Strackharn, E. M. Puchner, and H. E. Gaub, “Ultrastable combined atomic force and total internal reflection fluorescence microscope [corrected],” Rev. Sci. Instrum. 80(6), 063704 (2009).
[CrossRef] [PubMed]

R. A. Lugmaier, T. Hugel, M. Benoit, and H. E. Gaub, “Phase contrast and DIC illumination for AFM hybrids,” Ultramicroscopy 104(3-4), 255–260 (2005).
[CrossRef] [PubMed]

F. Oesterhelt, D. Oesterhelt, M. Pfeiffer, A. Engel, H. E. Gaub, and D. J. Müller, “Unfolding pathways of individual bacteriorhodopsins,” Science 288(5463), 143–146 (2000).
[CrossRef] [PubMed]

M. Rief, M. Gautel, F. Oesterhelt, J. M. Fernandez, and H. E. Gaub, “Reversible unfolding of individual titin immunoglobulin domains by AFM,” Science 276(5315), 1109–1112 (1997).
[CrossRef] [PubMed]

C. A. J. Putman, H. G. Hansma, H. E. Gaub, and P. K. Hansma, “Polymerized Lb Films Imaged with a Combined Atomic Force Microscope Fluorescence Microscope,” Langmuir 8(12), 3014–3019 (1992).
[CrossRef]

Gautel, M.

M. Rief, M. Gautel, F. Oesterhelt, J. M. Fernandez, and H. E. Gaub, “Reversible unfolding of individual titin immunoglobulin domains by AFM,” Science 276(5315), 1109–1112 (1997).
[CrossRef] [PubMed]

Gerber, C.

G. Binnig, C. F. Quate, and C. Gerber, “Atomic force microscope,” Phys. Rev. Lett. 56(9), 930–933 (1986).
[CrossRef] [PubMed]

Goldman, Y. E.

A. Yildiz, J. N. Forkey, S. A. McKinney, T. Ha, Y. E. Goldman, and P. R. Selvin, “Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization,” Science 300(5628), 2061–2065 (2003).
[CrossRef] [PubMed]

Gonçalves, R. P.

R. P. Gonçalves, G. Agnus, P. Sens, C. Houssin, B. Bartenlian, and S. Scheuring, “Two-chamber AFM: probing membrane proteins separating two aqueous compartments,” Nat. Methods 3(12), 1007–1012 (2006).
[CrossRef] [PubMed]

Gumpp, H.

H. Gumpp, S. W. Stahl, M. Strackharn, E. M. Puchner, and H. E. Gaub, “Ultrastable combined atomic force and total internal reflection fluorescence microscope [corrected],” Rev. Sci. Instrum. 80(6), 063704 (2009).
[CrossRef] [PubMed]

Ha, T.

A. Yildiz, J. N. Forkey, S. A. McKinney, T. Ha, Y. E. Goldman, and P. R. Selvin, “Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization,” Science 300(5628), 2061–2065 (2003).
[CrossRef] [PubMed]

Halsey, W.

Hansma, H. G.

C. A. J. Putman, H. G. Hansma, H. E. Gaub, and P. K. Hansma, “Polymerized Lb Films Imaged with a Combined Atomic Force Microscope Fluorescence Microscope,” Langmuir 8(12), 3014–3019 (1992).
[CrossRef]

Hansma, P. K.

C. A. J. Putman, H. G. Hansma, H. E. Gaub, and P. K. Hansma, “Polymerized Lb Films Imaged with a Combined Atomic Force Microscope Fluorescence Microscope,” Langmuir 8(12), 3014–3019 (1992).
[CrossRef]

Helenius, A.

H. Ewers, V. Jacobsen, E. Klotzsch, A. E. Smith, A. Helenius, and V. Sandoghdar, “Label-free optical detection and tracking of single virions bound to their receptors in supported membrane bilayers,” Nano Lett. 7(8), 2263–2266 (2007).
[CrossRef] [PubMed]

Hidaka, Y.

Y. Shichida, S. Matuoka, Y. Hidaka, and T. Yoshizawa, “Absorption spectra of intermediate of bacteriorhodopsin measured by laser photolysis at room temperatures,” Biochim. Biophys. Acta 723(2), 240–246 (1983).
[CrossRef]

Houssin, C.

R. P. Gonçalves, G. Agnus, P. Sens, C. Houssin, B. Bartenlian, and S. Scheuring, “Two-chamber AFM: probing membrane proteins separating two aqueous compartments,” Nat. Methods 3(12), 1007–1012 (2006).
[CrossRef] [PubMed]

Hugel, T.

R. A. Lugmaier, T. Hugel, M. Benoit, and H. E. Gaub, “Phase contrast and DIC illumination for AFM hybrids,” Ultramicroscopy 104(3-4), 255–260 (2005).
[CrossRef] [PubMed]

Jacobsen, V.

H. Ewers, V. Jacobsen, E. Klotzsch, A. E. Smith, A. Helenius, and V. Sandoghdar, “Label-free optical detection and tracking of single virions bound to their receptors in supported membrane bilayers,” Nano Lett. 7(8), 2263–2266 (2007).
[CrossRef] [PubMed]

V. Jacobsen, P. Stoller, C. Brunner, V. Vogel, and V. Sandoghdar, “Interferometric optical detection and tracking of very small gold nanoparticles at a water-glass interface,” Opt. Express 14(1), 405–414 (2006).
[CrossRef] [PubMed]

King, G. M.

Klotzsch, E.

H. Ewers, V. Jacobsen, E. Klotzsch, A. E. Smith, A. Helenius, and V. Sandoghdar, “Label-free optical detection and tracking of single virions bound to their receptors in supported membrane bilayers,” Nano Lett. 7(8), 2263–2266 (2007).
[CrossRef] [PubMed]

Kuwano, H.

H. Yamada, H. Tokumoto, S. Akamine, K. Fukuzawa, and H. Kuwano, “Imaging of organic molecular films using a scanning near-field optical microscope combined with an atomic force microscope,” J. Vac. Sci. Technol. B 14(2), 812–815 (1996).
[CrossRef]

Lieber, C. M.

C. D. Frisbie, L. F. Rozsnyai, A. Noy, M. S. Wrighton, and C. M. Lieber, “Functional group imaging by chemical force microscopy,” Science 265(5181), 2071–2074 (1994).
[CrossRef] [PubMed]

Lugmaier, R. A.

R. A. Lugmaier, T. Hugel, M. Benoit, and H. E. Gaub, “Phase contrast and DIC illumination for AFM hybrids,” Ultramicroscopy 104(3-4), 255–260 (2005).
[CrossRef] [PubMed]

Lukács, A.

A. Lukács, G. Garab, and E. Papp, “Measurement of the optical parameters of purple membrane and plant light-harvesting complex films with optical waveguide lightmode spectroscopy,” Biosens. Bioelectron. 21(8), 1606–1612 (2006).
[CrossRef] [PubMed]

Mathur, A. B.

A. B. Mathur, G. A. Truskey, and W. M. Reichert, “Atomic force and total internal reflection fluorescence microscopy for the study of force transmission in endothelial cells,” Biophys. J. 78(4), 1725–1735 (2000).
[CrossRef] [PubMed]

Matuoka, S.

Y. Shichida, S. Matuoka, Y. Hidaka, and T. Yoshizawa, “Absorption spectra of intermediate of bacteriorhodopsin measured by laser photolysis at room temperatures,” Biochim. Biophys. Acta 723(2), 240–246 (1983).
[CrossRef]

McKinney, S. A.

A. Yildiz, J. N. Forkey, S. A. McKinney, T. Ha, Y. E. Goldman, and P. R. Selvin, “Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization,” Science 300(5628), 2061–2065 (2003).
[CrossRef] [PubMed]

Meyer, G.

G. Meyer and N. M. Amer, “Novel Optical Approach to Atomic Force Microscopy,” Appl. Phys. Lett. 53(12), 1045–1047 (1988).
[CrossRef]

Michel, H.

H. Michel and D. Oesterhelt, “Three-dimensional crystals of membrane proteins: bacteriorhodopsin,” Proc. Natl. Acad. Sci. U.S.A. 77(3), 1283–1285 (1980).
[CrossRef] [PubMed]

Müller, D. J.

D. J. Müller and A. Engel, “Atomic force microscopy and spectroscopy of native membrane proteins,” Nat. Protoc. 2(9), 2191–2197 (2007).
[CrossRef] [PubMed]

F. Oesterhelt, D. Oesterhelt, M. Pfeiffer, A. Engel, H. E. Gaub, and D. J. Müller, “Unfolding pathways of individual bacteriorhodopsins,” Science 288(5463), 143–146 (2000).
[CrossRef] [PubMed]

D. J. Müller and A. Engel, “The height of biomolecules measured with the atomic force microscope depends on electrostatic interactions,” Biophys. J. 73(3), 1633–1644 (1997).
[CrossRef] [PubMed]

Noy, A.

C. D. Frisbie, L. F. Rozsnyai, A. Noy, M. S. Wrighton, and C. M. Lieber, “Functional group imaging by chemical force microscopy,” Science 265(5181), 2071–2074 (1994).
[CrossRef] [PubMed]

Oesterhelt, D.

F. Oesterhelt, D. Oesterhelt, M. Pfeiffer, A. Engel, H. E. Gaub, and D. J. Müller, “Unfolding pathways of individual bacteriorhodopsins,” Science 288(5463), 143–146 (2000).
[CrossRef] [PubMed]

H. Michel and D. Oesterhelt, “Three-dimensional crystals of membrane proteins: bacteriorhodopsin,” Proc. Natl. Acad. Sci. U.S.A. 77(3), 1283–1285 (1980).
[CrossRef] [PubMed]

Oesterhelt, F.

F. Oesterhelt, D. Oesterhelt, M. Pfeiffer, A. Engel, H. E. Gaub, and D. J. Müller, “Unfolding pathways of individual bacteriorhodopsins,” Science 288(5463), 143–146 (2000).
[CrossRef] [PubMed]

M. Rief, M. Gautel, F. Oesterhelt, J. M. Fernandez, and H. E. Gaub, “Reversible unfolding of individual titin immunoglobulin domains by AFM,” Science 276(5315), 1109–1112 (1997).
[CrossRef] [PubMed]

Papp, E.

A. Lukács, G. Garab, and E. Papp, “Measurement of the optical parameters of purple membrane and plant light-harvesting complex films with optical waveguide lightmode spectroscopy,” Biosens. Bioelectron. 21(8), 1606–1612 (2006).
[CrossRef] [PubMed]

Perkins, T. T.

Pfeiffer, M.

F. Oesterhelt, D. Oesterhelt, M. Pfeiffer, A. Engel, H. E. Gaub, and D. J. Müller, “Unfolding pathways of individual bacteriorhodopsins,” Science 288(5463), 143–146 (2000).
[CrossRef] [PubMed]

Puchner, E. M.

H. Gumpp, S. W. Stahl, M. Strackharn, E. M. Puchner, and H. E. Gaub, “Ultrastable combined atomic force and total internal reflection fluorescence microscope [corrected],” Rev. Sci. Instrum. 80(6), 063704 (2009).
[CrossRef] [PubMed]

Putman, C. A. J.

C. A. J. Putman, H. G. Hansma, H. E. Gaub, and P. K. Hansma, “Polymerized Lb Films Imaged with a Combined Atomic Force Microscope Fluorescence Microscope,” Langmuir 8(12), 3014–3019 (1992).
[CrossRef]

Quate, C. F.

G. Binnig, C. F. Quate, and C. Gerber, “Atomic force microscope,” Phys. Rev. Lett. 56(9), 930–933 (1986).
[CrossRef] [PubMed]

Reichert, W. M.

A. B. Mathur, G. A. Truskey, and W. M. Reichert, “Atomic force and total internal reflection fluorescence microscopy for the study of force transmission in endothelial cells,” Biophys. J. 78(4), 1725–1735 (2000).
[CrossRef] [PubMed]

Rief, M.

M. Rief, M. Gautel, F. Oesterhelt, J. M. Fernandez, and H. E. Gaub, “Reversible unfolding of individual titin immunoglobulin domains by AFM,” Science 276(5315), 1109–1112 (1997).
[CrossRef] [PubMed]

Rozsnyai, L. F.

C. D. Frisbie, L. F. Rozsnyai, A. Noy, M. S. Wrighton, and C. M. Lieber, “Functional group imaging by chemical force microscopy,” Science 265(5181), 2071–2074 (1994).
[CrossRef] [PubMed]

Sandoghdar, V.

H. Ewers, V. Jacobsen, E. Klotzsch, A. E. Smith, A. Helenius, and V. Sandoghdar, “Label-free optical detection and tracking of single virions bound to their receptors in supported membrane bilayers,” Nano Lett. 7(8), 2263–2266 (2007).
[CrossRef] [PubMed]

V. Jacobsen, P. Stoller, C. Brunner, V. Vogel, and V. Sandoghdar, “Interferometric optical detection and tracking of very small gold nanoparticles at a water-glass interface,” Opt. Express 14(1), 405–414 (2006).
[CrossRef] [PubMed]

Scheuring, S.

R. P. Gonçalves, G. Agnus, P. Sens, C. Houssin, B. Bartenlian, and S. Scheuring, “Two-chamber AFM: probing membrane proteins separating two aqueous compartments,” Nat. Methods 3(12), 1007–1012 (2006).
[CrossRef] [PubMed]

S. Scheuring and J. N. Sturgis, “Chromatic adaptation of photosynthetic membranes,” Science 309(5733), 484–487 (2005).
[CrossRef] [PubMed]

Selvin, P. R.

A. Yildiz, J. N. Forkey, S. A. McKinney, T. Ha, Y. E. Goldman, and P. R. Selvin, “Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization,” Science 300(5628), 2061–2065 (2003).
[CrossRef] [PubMed]

Sens, P.

R. P. Gonçalves, G. Agnus, P. Sens, C. Houssin, B. Bartenlian, and S. Scheuring, “Two-chamber AFM: probing membrane proteins separating two aqueous compartments,” Nat. Methods 3(12), 1007–1012 (2006).
[CrossRef] [PubMed]

Shichida, Y.

Y. Shichida, S. Matuoka, Y. Hidaka, and T. Yoshizawa, “Absorption spectra of intermediate of bacteriorhodopsin measured by laser photolysis at room temperatures,” Biochim. Biophys. Acta 723(2), 240–246 (1983).
[CrossRef]

Smith, A. E.

H. Ewers, V. Jacobsen, E. Klotzsch, A. E. Smith, A. Helenius, and V. Sandoghdar, “Label-free optical detection and tracking of single virions bound to their receptors in supported membrane bilayers,” Nano Lett. 7(8), 2263–2266 (2007).
[CrossRef] [PubMed]

Stahl, S. W.

H. Gumpp, S. W. Stahl, M. Strackharn, E. M. Puchner, and H. E. Gaub, “Ultrastable combined atomic force and total internal reflection fluorescence microscope [corrected],” Rev. Sci. Instrum. 80(6), 063704 (2009).
[CrossRef] [PubMed]

Stoller, P.

Strackharn, M.

H. Gumpp, S. W. Stahl, M. Strackharn, E. M. Puchner, and H. E. Gaub, “Ultrastable combined atomic force and total internal reflection fluorescence microscope [corrected],” Rev. Sci. Instrum. 80(6), 063704 (2009).
[CrossRef] [PubMed]

Sturgis, J. N.

S. Scheuring and J. N. Sturgis, “Chromatic adaptation of photosynthetic membranes,” Science 309(5733), 484–487 (2005).
[CrossRef] [PubMed]

Tokumoto, H.

H. Yamada, H. Tokumoto, S. Akamine, K. Fukuzawa, and H. Kuwano, “Imaging of organic molecular films using a scanning near-field optical microscope combined with an atomic force microscope,” J. Vac. Sci. Technol. B 14(2), 812–815 (1996).
[CrossRef]

Truskey, G. A.

A. B. Mathur, G. A. Truskey, and W. M. Reichert, “Atomic force and total internal reflection fluorescence microscopy for the study of force transmission in endothelial cells,” Biophys. J. 78(4), 1725–1735 (2000).
[CrossRef] [PubMed]

Ulrich, T. A.

Vogel, V.

Wrighton, M. S.

C. D. Frisbie, L. F. Rozsnyai, A. Noy, M. S. Wrighton, and C. M. Lieber, “Functional group imaging by chemical force microscopy,” Science 265(5181), 2071–2074 (1994).
[CrossRef] [PubMed]

Yamada, H.

H. Yamada, H. Tokumoto, S. Akamine, K. Fukuzawa, and H. Kuwano, “Imaging of organic molecular films using a scanning near-field optical microscope combined with an atomic force microscope,” J. Vac. Sci. Technol. B 14(2), 812–815 (1996).
[CrossRef]

Yildiz, A.

A. Yildiz, J. N. Forkey, S. A. McKinney, T. Ha, Y. E. Goldman, and P. R. Selvin, “Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization,” Science 300(5628), 2061–2065 (2003).
[CrossRef] [PubMed]

Yoshizawa, T.

Y. Shichida, S. Matuoka, Y. Hidaka, and T. Yoshizawa, “Absorption spectra of intermediate of bacteriorhodopsin measured by laser photolysis at room temperatures,” Biochim. Biophys. Acta 723(2), 240–246 (1983).
[CrossRef]

Appl. Opt. (1)

Appl. Phys. Lett. (1)

G. Meyer and N. M. Amer, “Novel Optical Approach to Atomic Force Microscopy,” Appl. Phys. Lett. 53(12), 1045–1047 (1988).
[CrossRef]

Biochim. Biophys. Acta (1)

Y. Shichida, S. Matuoka, Y. Hidaka, and T. Yoshizawa, “Absorption spectra of intermediate of bacteriorhodopsin measured by laser photolysis at room temperatures,” Biochim. Biophys. Acta 723(2), 240–246 (1983).
[CrossRef]

Biophys. J. (2)

D. J. Müller and A. Engel, “The height of biomolecules measured with the atomic force microscope depends on electrostatic interactions,” Biophys. J. 73(3), 1633–1644 (1997).
[CrossRef] [PubMed]

A. B. Mathur, G. A. Truskey, and W. M. Reichert, “Atomic force and total internal reflection fluorescence microscopy for the study of force transmission in endothelial cells,” Biophys. J. 78(4), 1725–1735 (2000).
[CrossRef] [PubMed]

Biosens. Bioelectron. (1)

A. Lukács, G. Garab, and E. Papp, “Measurement of the optical parameters of purple membrane and plant light-harvesting complex films with optical waveguide lightmode spectroscopy,” Biosens. Bioelectron. 21(8), 1606–1612 (2006).
[CrossRef] [PubMed]

J. Bacteriol. (1)

S. M. Block, K. A. Fahrner, and H. C. Berg, “Visualization of bacterial flagella by video-enhanced light microscopy,” J. Bacteriol. 173(2), 933–936 (1991).
[PubMed]

J. Vac. Sci. Technol. B (1)

H. Yamada, H. Tokumoto, S. Akamine, K. Fukuzawa, and H. Kuwano, “Imaging of organic molecular films using a scanning near-field optical microscope combined with an atomic force microscope,” J. Vac. Sci. Technol. B 14(2), 812–815 (1996).
[CrossRef]

Langmuir (1)

C. A. J. Putman, H. G. Hansma, H. E. Gaub, and P. K. Hansma, “Polymerized Lb Films Imaged with a Combined Atomic Force Microscope Fluorescence Microscope,” Langmuir 8(12), 3014–3019 (1992).
[CrossRef]

Nano Lett. (2)

H. Ewers, V. Jacobsen, E. Klotzsch, A. E. Smith, A. Helenius, and V. Sandoghdar, “Label-free optical detection and tracking of single virions bound to their receptors in supported membrane bilayers,” Nano Lett. 7(8), 2263–2266 (2007).
[CrossRef] [PubMed]

G. M. King, A. R. Carter, A. B. Churnside, L. S. Eberle, and T. T. Perkins, “Ultrastable atomic force microscopy: atomic-scale lateral stability and registration in ambient condition,” Nano Lett. 9(4), 1451–1456 (2009).
[CrossRef] [PubMed]

Nat. Methods (1)

R. P. Gonçalves, G. Agnus, P. Sens, C. Houssin, B. Bartenlian, and S. Scheuring, “Two-chamber AFM: probing membrane proteins separating two aqueous compartments,” Nat. Methods 3(12), 1007–1012 (2006).
[CrossRef] [PubMed]

Nat. Protoc. (1)

D. J. Müller and A. Engel, “Atomic force microscopy and spectroscopy of native membrane proteins,” Nat. Protoc. 2(9), 2191–2197 (2007).
[CrossRef] [PubMed]

Opt. Express (2)

Phys. Rev. Lett. (1)

G. Binnig, C. F. Quate, and C. Gerber, “Atomic force microscope,” Phys. Rev. Lett. 56(9), 930–933 (1986).
[CrossRef] [PubMed]

Proc. Natl. Acad. Sci. U.S.A. (1)

H. Michel and D. Oesterhelt, “Three-dimensional crystals of membrane proteins: bacteriorhodopsin,” Proc. Natl. Acad. Sci. U.S.A. 77(3), 1283–1285 (1980).
[CrossRef] [PubMed]

Rev. Sci. Instrum. (1)

H. Gumpp, S. W. Stahl, M. Strackharn, E. M. Puchner, and H. E. Gaub, “Ultrastable combined atomic force and total internal reflection fluorescence microscope [corrected],” Rev. Sci. Instrum. 80(6), 063704 (2009).
[CrossRef] [PubMed]

Science (5)

A. Yildiz, J. N. Forkey, S. A. McKinney, T. Ha, Y. E. Goldman, and P. R. Selvin, “Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization,” Science 300(5628), 2061–2065 (2003).
[CrossRef] [PubMed]

M. Rief, M. Gautel, F. Oesterhelt, J. M. Fernandez, and H. E. Gaub, “Reversible unfolding of individual titin immunoglobulin domains by AFM,” Science 276(5315), 1109–1112 (1997).
[CrossRef] [PubMed]

S. Scheuring and J. N. Sturgis, “Chromatic adaptation of photosynthetic membranes,” Science 309(5733), 484–487 (2005).
[CrossRef] [PubMed]

C. D. Frisbie, L. F. Rozsnyai, A. Noy, M. S. Wrighton, and C. M. Lieber, “Functional group imaging by chemical force microscopy,” Science 265(5181), 2071–2074 (1994).
[CrossRef] [PubMed]

F. Oesterhelt, D. Oesterhelt, M. Pfeiffer, A. Engel, H. E. Gaub, and D. J. Müller, “Unfolding pathways of individual bacteriorhodopsins,” Science 288(5463), 143–146 (2000).
[CrossRef] [PubMed]

Ultramicroscopy (1)

R. A. Lugmaier, T. Hugel, M. Benoit, and H. E. Gaub, “Phase contrast and DIC illumination for AFM hybrids,” Ultramicroscopy 104(3-4), 255–260 (2005).
[CrossRef] [PubMed]

Other (1)

D. J. Griffiths, Introduction to Electrodynamics (Prentice Hall, Upper Saddle River, NJ, 1999).

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