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]
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]
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]
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]
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]
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]
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]
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]
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]
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]
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]
G. Meyer and N. M. Amer, “Novel Optical Approach to Atomic Force Microscopy,” Appl. Phys. Lett. 53(12), 1045–1047 (1988).
[Crossref]
G. Binnig, C. F. Quate, and C. Gerber, “Atomic force microscope,” Phys. Rev. Lett. 56(9), 930–933 (1986).
[Crossref]
[PubMed]
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]
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]
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]
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]
G. Meyer and N. M. Amer, “Novel Optical Approach to Atomic Force Microscopy,” Appl. Phys. Lett. 53(12), 1045–1047 (1988).
[Crossref]
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]
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]
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]
G. Binnig, C. F. Quate, and C. Gerber, “Atomic force microscope,” Phys. Rev. Lett. 56(9), 930–933 (1986).
[Crossref]
[PubMed]
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]
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]
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]
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]
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]
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]
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]
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]
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]
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]
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]
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]
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]
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]
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]
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]
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]
G. Binnig, C. F. Quate, and C. Gerber, “Atomic force microscope,” Phys. Rev. Lett. 56(9), 930–933 (1986).
[Crossref]
[PubMed]
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]
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]
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]
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]
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]
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]
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]
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]
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]
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]
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]
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]
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]
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]
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]
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]
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]
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]
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]
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]
G. Meyer and N. M. Amer, “Novel Optical Approach to Atomic Force Microscopy,” Appl. Phys. Lett. 53(12), 1045–1047 (1988).
[Crossref]
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]
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]
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]
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]
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]
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]
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]
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]
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]
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]
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]
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]
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]
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]
G. Binnig, C. F. Quate, and C. Gerber, “Atomic force microscope,” Phys. Rev. Lett. 56(9), 930–933 (1986).
[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]
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. 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]
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]
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]
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]
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]
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]
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]
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]
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]
S. Scheuring and J. N. Sturgis, “Chromatic adaptation of photosynthetic membranes,” Science 309(5733), 484–487 (2005).
[Crossref]
[PubMed]
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]
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]
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]
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]
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]
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]
G. Meyer and N. M. Amer, “Novel Optical Approach to Atomic Force Microscopy,” Appl. Phys. Lett. 53(12), 1045–1047 (1988).
[Crossref]
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]
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]
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]
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]
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]
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]
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]
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]
D. J. Müller and A. Engel, “Atomic force microscopy and spectroscopy of native membrane proteins,” Nat. Protoc. 2(9), 2191–2197 (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]
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]
G. Binnig, C. F. Quate, and C. Gerber, “Atomic force microscope,” Phys. Rev. Lett. 56(9), 930–933 (1986).
[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]
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]
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]
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]
D. J. Griffiths, Introduction to Electrodynamics (Prentice Hall, Upper Saddle River, NJ, 1999).