IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v594y2021i7863d10.1038_s41586-021-03551-x.html
   My bibliography  Save this article

Localization atomic force microscopy

Author

Listed:
  • George R. Heath

    (Weill Cornell Medicine
    University of Leeds)

  • Ekaterina Kots

    (Weill Cornell Medicine)

  • Janice L. Robertson

    (Washington University)

  • Shifra Lansky

    (Weill Cornell Medicine)

  • George Khelashvili

    (Weill Cornell Medicine)

  • Harel Weinstein

    (Weill Cornell Medicine)

  • Simon Scheuring

    (Weill Cornell Medicine
    Weill Cornell Medicine)

Abstract

Understanding structural dynamics of biomolecules at the single-molecule level is vital to advancing our knowledge of molecular mechanisms. Currently, there are few techniques that can capture dynamics at the sub-nanometre scale and in physiologically relevant conditions. Atomic force microscopy (AFM)1 has the advantage of analysing unlabelled single molecules in physiological buffer and at ambient temperature and pressure, but its resolution limits the assessment of conformational details of biomolecules2. Here we present localization AFM (LAFM), a technique developed to overcome current resolution limitations. By applying localization image reconstruction algorithms3 to peak positions in high-speed AFM and conventional AFM data, we increase the resolution beyond the limits set by the tip radius, and resolve single amino acid residues on soft protein surfaces in native and dynamic conditions. LAFM enables the calculation of high-resolution maps from either images of many molecules or many images of a single molecule acquired over time, facilitating single-molecule structural analysis. LAFM is a post-acquisition image reconstruction method that can be applied to any biomolecular AFM dataset.

Suggested Citation

  • George R. Heath & Ekaterina Kots & Janice L. Robertson & Shifra Lansky & George Khelashvili & Harel Weinstein & Simon Scheuring, 2021. "Localization atomic force microscopy," Nature, Nature, vol. 594(7863), pages 385-390, June.
    • Handle: RePEc:nat:nature:v:594:y:2021:i:7863:d:10.1038_s41586-021-03551-x
    DOI: 10.1038/s41586-021-03551-x
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41586-021-03551-x
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/s41586-021-03551-x?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Jienyu Ding & Yun-Tzai Lee & Yuba Bhandari & Charles D. Schwieters & Lixin Fan & Ping Yu & Sergey G. Tarosov & Jason R. Stagno & Buyong Ma & Ruth Nussinov & Alan Rein & Jinwei Zhang & Yun-Xing Wang, 2023. "Visualizing RNA conformational and architectural heterogeneity in solution," Nature Communications, Nature, vol. 14(1), pages 1-11, December.
    2. Alma P. Perrino & Atsushi Miyagi & Simon Scheuring, 2021. "Single molecule kinetics of bacteriorhodopsin by HS-AFM," Nature Communications, Nature, vol. 12(1), pages 1-10, December.
    3. Yining Jiang & Batiste Thienpont & Vinay Sapuru & Richard K. Hite & Jeremy S. Dittman & James N. Sturgis & Simon Scheuring, 2022. "Membrane-mediated protein interactions drive membrane protein organization," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    4. Fang Jiao & François Dehez & Tao Ni & Xiulian Yu & Jeremy S. Dittman & Robert Gilbert & Christophe Chipot & Simon Scheuring, 2022. "Perforin-2 clockwise hand-over-hand pre-pore to pore transition mechanism," Nature Communications, Nature, vol. 13(1), pages 1-13, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:594:y:2021:i:7863:d:10.1038_s41586-021-03551-x. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.