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double helix point spread function  (Double Helix)

 
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    Double Helix double helix point spread function
    Double Helix Point Spread Function, supplied by Double Helix, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/double-helix+point+spread+function/double+function+helix+point+spread/pm42275202-302-40-40
    Average 86 stars, based on 1 article reviews
    double helix point spread function - by Bioz Stars, 2026-11
    86/100 stars

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    Related Articles

    Microscopy:

    Article Title: Quantum-inspired super-resolution of fluorescent point-like sources.
    Article Snippet: .. Backlund, M., Joyner, R., Weis, K. & Moerner, W. E. Correlations of three-dimensional motion of chromosomal loci in yeast revealed by the double-helix point spread function microscope. ..

    Article Title: Chromatin remodelling enables enhancer resetting to facilitate the ERK transcriptional response
    Article Snippet: .. Using a double helix point-spread function microscope we generated 3D tracks of individual HALO-tagged NANOG or SOX2 proteins in the nucleus. ..

    other:

    Article Title: Scale-Dependent Emergence of Hindered Diffusion in the Brain Extracellular Space
    Article Snippet: We therefore employ PSF engineering [56] to track uCCNTs in three dimensions using a double-helix point-spread function (DH-PSF) [57], as previously in [53].

    Fluorescence:

    Article Title: Scale-Dependent Emergence of Hindered Diffusion in the Brain Extracellular Space
    Article Snippet: .. [57] S. R. P. Pavani, M. A. Thompson, J. S. Biteen, S. J. Lord, N. Liu, R. J. Twieg, R. Piestun, and W. E. Moerner, Three-dimensional, single-molecule fluorescence imaging beyond the diffraction limit by using a double-helix point spread function, Proceedings of the National Academy of Sciences 106, 2995 (2009). ..

    Article Title: Versatile and Scalable Reflective Micromirrors for Single-Objective Light Sheet Microscopy.
    Article Snippet: .. Traffic 2001, 2 (11), 764−774. (69) Pavani, S. R. P.; Thompson, M. A.; Biteen, J. S.; Lord, S. J.; Liu, N.; Twieg, R. J.; Piestun, R.; Moerner, W. E. Three-Dimensional, Single-Molecule Fluorescence Imaging beyond the Diffraction Limit by Using a Double-Helix Point Spread Function. ..

    Imaging:

    Article Title: Scale-Dependent Emergence of Hindered Diffusion in the Brain Extracellular Space
    Article Snippet: .. [57] S. R. P. Pavani, M. A. Thompson, J. S. Biteen, S. J. Lord, N. Liu, R. J. Twieg, R. Piestun, and W. E. Moerner, Three-dimensional, single-molecule fluorescence imaging beyond the diffraction limit by using a double-helix point spread function, Proceedings of the National Academy of Sciences 106, 2995 (2009). ..

    Article Title: Early synaptic pathology is associated with small tau aggregates in Alzheimer's disease.
    Article Snippet: .. Three-dimensional (3D) super-resolution imaging of AT8positive tau in the synaptosome samples was performed using the double-helix (DH) point spread function technique to obtain precise 3D localisation information. ..

    Article Title: Versatile and Scalable Reflective Micromirrors for Single-Objective Light Sheet Microscopy.
    Article Snippet: .. U.S.A. 2009, 106 (9), 2995−2999. (70) Nakatani, Y.; Gaumer, S.; Shechtman, Y.; Gustavsson, A.-K. Long Axial-Range Double-Helix Point Spread Functions for 3D Volumetric Super-Resolution Imaging. ..

    Article Title: Versatile and Scalable Reflective Micromirrors for Single-Objective Light Sheet Microscopy.
    Article Snippet: .. Traffic 2001, 2 (11), 764−774. (69) Pavani, S. R. P.; Thompson, M. A.; Biteen, J. S.; Lord, S. J.; Liu, N.; Twieg, R. J.; Piestun, R.; Moerner, W. E. Three-Dimensional, Single-Molecule Fluorescence Imaging beyond the Diffraction Limit by Using a Double-Helix Point Spread Function. ..

    Generated:

    Article Title: Chromatin remodelling enables enhancer resetting to facilitate the ERK transcriptional response
    Article Snippet: .. Using a double helix point-spread function microscope we generated 3D tracks of individual HALO-tagged NANOG or SOX2 proteins in the nucleus. ..



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    A) Toxoplasma Gondii utilizes an apical complex to drive invasion of host cells. The conoid is a prominent feature of the apical complex. The precise organization of MyoH within the apical complex is unknown. B) Cryo-electron tomography has provided a density map of the conoid fibrils in situ (modified from Ref. ). C) The conoid fibrils are comprised of a comma-shaped arrangement of tubulin monomers with several conoid-associated proteins coating the tubulin. D) Two lines of parasite are created to label either terminus of MyoH, as indicated by the relative location of the red star on the miniaturized cartoon of a myosin monomer. MyoH-ALFA possesses a C-terminal fusion of the ALFA tag, while ALFA-MyoH possesses an N-terminal fusion. The ALFA tag is targeted by a nanobody conjugated to Alexa Fluor 647. E) <t>The</t> <t>Double-Helix</t> Point Spread Function <t>(DHPSF)</t> allows for scanning-free imaging of single-molecule fluorescence over a ∼2.5-μm axial range. Fluorophores (red stars 1, 2, and 3) have their z position encoded in the angle (θ) formed between the line bisecting the two lobes of the PSF (cyan) and the horizontal (dashed white). F) Gel expansion has been shown to increase protein accessibility, which is useful for the dense protein environment of the apical complex. Scale Bar: (E) 1 μm.
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    double helix point spread function dh psf  (Double Helix)
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    Double Helix double helix point spread function dh psf
    A) Toxoplasma Gondii utilizes an apical complex to drive invasion of host cells. The conoid is a prominent feature of the apical complex. The precise organization of MyoH within the apical complex is unknown. B) Cryo-electron tomography has provided a density map of the conoid fibrils in situ (modified from Ref. ). C) The conoid fibrils are comprised of a comma-shaped arrangement of tubulin monomers with several conoid-associated proteins coating the tubulin. D) Two lines of parasite are created to label either terminus of MyoH, as indicated by the relative location of the red star on the miniaturized cartoon of a myosin monomer. MyoH-ALFA possesses a C-terminal fusion of the ALFA tag, while ALFA-MyoH possesses an N-terminal fusion. The ALFA tag is targeted by a nanobody conjugated to Alexa Fluor 647. E) <t>The</t> <t>Double-Helix</t> Point Spread Function <t>(DHPSF)</t> allows for scanning-free imaging of single-molecule fluorescence over a ∼2.5-μm axial range. Fluorophores (red stars 1, 2, and 3) have their z position encoded in the angle (θ) formed between the line bisecting the two lobes of the PSF (cyan) and the horizontal (dashed white). F) Gel expansion has been shown to increase protein accessibility, which is useful for the dense protein environment of the apical complex. Scale Bar: (E) 1 μm.
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    double helix point spread functions  (Double Helix)
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    Double Helix double helix point spread functions
    A) Toxoplasma Gondii utilizes an apical complex to drive invasion of host cells. The conoid is a prominent feature of the apical complex. The precise organization of MyoH within the apical complex is unknown. B) Cryo-electron tomography has provided a density map of the conoid fibrils in situ (modified from Ref. ). C) The conoid fibrils are comprised of a comma-shaped arrangement of tubulin monomers with several conoid-associated proteins coating the tubulin. D) Two lines of parasite are created to label either terminus of MyoH, as indicated by the relative location of the red star on the miniaturized cartoon of a myosin monomer. MyoH-ALFA possesses a C-terminal fusion of the ALFA tag, while ALFA-MyoH possesses an N-terminal fusion. The ALFA tag is targeted by a nanobody conjugated to Alexa Fluor 647. E) <t>The</t> <t>Double-Helix</t> Point Spread Function <t>(DHPSF)</t> allows for scanning-free imaging of single-molecule fluorescence over a ∼2.5-μm axial range. Fluorophores (red stars 1, 2, and 3) have their z position encoded in the angle (θ) formed between the line bisecting the two lobes of the PSF (cyan) and the horizontal (dashed white). F) Gel expansion has been shown to increase protein accessibility, which is useful for the dense protein environment of the apical complex. Scale Bar: (E) 1 μm.
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    double helix point spread functions - by Bioz Stars, 2026-11
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    A) Toxoplasma Gondii utilizes an apical complex to drive invasion of host cells. The conoid is a prominent feature of the apical complex. The precise organization of MyoH within the apical complex is unknown. B) Cryo-electron tomography has provided a density map of the conoid fibrils in situ (modified from Ref. ). C) The conoid fibrils are comprised of a comma-shaped arrangement of tubulin monomers with several conoid-associated proteins coating the tubulin. D) Two lines of parasite are created to label either terminus of MyoH, as indicated by the relative location of the red star on the miniaturized cartoon of a myosin monomer. MyoH-ALFA possesses a C-terminal fusion of the ALFA tag, while ALFA-MyoH possesses an N-terminal fusion. The ALFA tag is targeted by a nanobody conjugated to Alexa Fluor 647. E) The Double-Helix Point Spread Function (DHPSF) allows for scanning-free imaging of single-molecule fluorescence over a ∼2.5-μm axial range. Fluorophores (red stars 1, 2, and 3) have their z position encoded in the angle (θ) formed between the line bisecting the two lobes of the PSF (cyan) and the horizontal (dashed white). F) Gel expansion has been shown to increase protein accessibility, which is useful for the dense protein environment of the apical complex. Scale Bar: (E) 1 μm.

    Journal: bioRxiv

    Article Title: Organization of Myosin H in the Apical Complex of Toxoplasma Gondii Revealed by 3D Single-Molecule Super-Resolution Microscopy

    doi: 10.64898/2026.04.23.720434

    Figure Lengend Snippet: A) Toxoplasma Gondii utilizes an apical complex to drive invasion of host cells. The conoid is a prominent feature of the apical complex. The precise organization of MyoH within the apical complex is unknown. B) Cryo-electron tomography has provided a density map of the conoid fibrils in situ (modified from Ref. ). C) The conoid fibrils are comprised of a comma-shaped arrangement of tubulin monomers with several conoid-associated proteins coating the tubulin. D) Two lines of parasite are created to label either terminus of MyoH, as indicated by the relative location of the red star on the miniaturized cartoon of a myosin monomer. MyoH-ALFA possesses a C-terminal fusion of the ALFA tag, while ALFA-MyoH possesses an N-terminal fusion. The ALFA tag is targeted by a nanobody conjugated to Alexa Fluor 647. E) The Double-Helix Point Spread Function (DHPSF) allows for scanning-free imaging of single-molecule fluorescence over a ∼2.5-μm axial range. Fluorophores (red stars 1, 2, and 3) have their z position encoded in the angle (θ) formed between the line bisecting the two lobes of the PSF (cyan) and the horizontal (dashed white). F) Gel expansion has been shown to increase protein accessibility, which is useful for the dense protein environment of the apical complex. Scale Bar: (E) 1 μm.

    Article Snippet: We used the double-helix point spread function (DHPSF) and (d)STORM-style blinking ( , ) to localize single MyoH molecules in 3D with high-precision (AF647: 12 nm lateral, 20 nm axial; CF583R: 27 nm lateral, 40 nm axial; Fig. S4) across a 2.5-μm axial range ( , ).

    Techniques: Tomography, In Situ, Modification, Imaging, Fluorescence