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a k long axial range double helix point spread functions  (Double Helix)

 
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    Double Helix a k long axial range double helix point spread functions
    A K Long Axial Range Double Helix Point Spread Functions, 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/pm42275202-307-13-16
    Average 86 stars, based on 1 article reviews
    a k long axial range double helix point spread functions - by Bioz Stars, 2026-11
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    other:

    Article Title: 3D Super-Resolution Imaging of PSD95 Reveals an Abundance of Diffuse Protein Supercomplexes in the Mouse Brain.
    Article Snippet: 2024, 15 (1), No. 1940. (36) Carr, A. R.; Ponjavic, A.; Basu, S.; McColl, J.; Santos, A. M.; Davis, S.; Laue, E. D.; Klenerman, D.; Lee, S. F. Three-Dimensional Super-Resolution in Eukaryotic Cells Using the Double-Helix Point Spread Function.

    Article Title: 3D Super-Resolution Imaging of PSD95 Reveals an Abundance of Diffuse Protein Supercomplexes in the Mouse Brain.
    Article Snippet: Science 2008, 319 (5864), 810−813. (31) Backlund, M. P.; Lew, M. D.; Backer, A. S.; Sahl, S. J.; Grover, G.; Agrawal, A.; Piestun, R.; Moerner, W. E. In The Double-Helix Point Spread Function Enables Precise and Accurate Measurement of 3D SingleMolecule Localization and Orientation, Single Molecule Spectroscopy and Superresolution Imaging VI; SPIE, 2013; p 85900. (32) Gustavsson, A. K.; Petrov, P. N.; Lee, M. Y.; Shechtman, Y.; Moerner, W. E. 3D Single-Molecule Super-Resolution Microscopy with a Tilted Light Sheet.

    Article Title: 3D Super-Resolution Imaging of PSD95 Reveals an Abundance of Diffuse Protein Supercomplexes in the Mouse Brain.
    Article Snippet: 2013 DOI: 10.1038/protex.2013.026. (49) Carr, A. R.; Ponjavic, A.; Basu, S.; McColl, J.; Santos, A. M.; Davis, S.; Laue, E. D.; Klenerman, D.; Lee, S. F. Three-Dimensional Super-Resolution in Eukaryotic Cells Using the Double-Helix Point Spread Function.

    Article Title: Long-Axial-Range Double-Helix Point Spread Functions for 3D Volumetric Super-Resolution Imaging.
    Article Snippet: Express 2024, 15 (5), 3050−3063. (37) Thompson, M. A.; Casolari, J. M.; Badieirostami, M.; Brown, P. O.; Moerner, W. E. Three-Dimensional Tracking of Single mRNA Particles in Saccharomyces Cerevisiae Using a Double-Helix Point Spread Function.

    Article Title: 3D Super-Resolution Imaging of PSD95 Reveals an Abundance of Diffuse Protein Supercomplexes in the Mouse Brain.
    Article Snippet: 2017, 112 (7), 1444−1454. (37) Badieirostami, M.; Lew, M. D.; Thompson, M. A.; Moerner, W. E. Three-Dimensional Localization Precision of the Double-Helix Point Spread Function versus Astigmatism and Biplane.

    Article Title: 3D Super-Resolution Imaging of PSD95 Reveals an Abundance of Diffuse Protein Supercomplexes in the Mouse Brain
    Article Snippet: 2014, 63 (3), 227–234. https://doi.org/10.1093/jmicro/dfu006. (5) Carr, A. R.; Ponjavic, A.; Basu, S.; McColl, J.; Santos, A. M.; Davis, S.; Laue, E. D.; Klenerman, D.; Lee, S. F. Three- Dimensional Super-Resolution in Eukaryotic Cells Using the Double-Helix Point Spread Function.

    Fluorescence:

    Article Title: Dark tracking, hybrid method, conical diffraction microscopy and dark addressing
    Article Snippet: .. “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 (9): 2995-2999. .. Reymond, L., J. Ziegler, C. Knapp, F.-C. Wang, T. Huser, V. Ruprecht and S. Wieser (2019).

    Article Title: Dual-Bessel-Beam Stimulated Emission Depletion Microscopy for Super-resolution Volumetric Projection Imaging of Lipid Droplet Dynamics.
    Article Snippet: Volumetric imaging efficiently captures comprehensive spatial structures and dynamic function information on organisms in biomedical research.. However, optical diffraction limit restricts the visualization of fine structure details at nanoscale.. To address this limitation, we developed dual-Bessel-beam stimulated emission depletion (DB-STED) microscopy to enhance the information throughput and lateral resolution.

    Imaging:

    Article Title: Dark tracking, hybrid method, conical diffraction microscopy and dark addressing
    Article Snippet: .. “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 (9): 2995-2999. .. Reymond, L., J. Ziegler, C. Knapp, F.-C. Wang, T. Huser, V. Ruprecht and S. Wieser (2019).

    Article Title: Dual-Bessel-Beam Stimulated Emission Depletion Microscopy for Super-resolution Volumetric Projection Imaging of Lipid Droplet Dynamics.
    Article Snippet: Volumetric imaging efficiently captures comprehensive spatial structures and dynamic function information on organisms in biomedical research.. However, optical diffraction limit restricts the visualization of fine structure details at nanoscale.. To address this limitation, we developed dual-Bessel-beam stimulated emission depletion (DB-STED) microscopy to enhance the information throughput and lateral resolution.



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    a k long axial range double helix point spread functions  (Double Helix)
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    Double Helix a k long axial range double helix point spread functions
    A K Long Axial Range Double Helix Point Spread Functions, 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/pm42275202-307-13-16
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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
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    double helix point spread function dhpsf  (Double Helix)
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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.
    Double Helix Point Spread Function Dhpsf, 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/bio_rxiv__64898__2026__04__23__720434-44-3-3
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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.
    Double Helix Point Spread Function Dh Psf, 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/arxiv__2603__18936-54-14-14
    Average 86 stars, based on 1 article reviews
    double helix point spread function dh psf - by Bioz Stars, 2026-11
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    double helix point spread functions  (Double Helix)
    86
    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.
    Double Helix Point Spread Functions, 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/bio_rxiv__2025__08__14__670427-0-9-9
    Average 86 stars, based on 1 article reviews
    double helix point spread functions - by Bioz Stars, 2026-11
    86/100 stars
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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