University Library
  • Login
A gateway to Melbourne's research publications
Minerva Access is the University's Institutional Repository. It aims to collect, preserve, and showcase the intellectual output of staff and students of the University of Melbourne for a global audience.
View Item 
  • Minerva Access
  • Science
  • School of Physics
  • School of Physics - Research Publications
  • View Item
  • Minerva Access
  • Science
  • School of Physics
  • School of Physics - Research Publications
  • View Item
JavaScript is disabled for your browser. Some features of this site may not work without it.

    Structural Heterogeneity in Single Particle Imaging Using X-ray Lasers

    Thumbnail
    Download
    Published version (3.078Mb)

    Citations
    Scopus
    Altmetric
    1
    Author
    Mandl, T; Ostlin, C; Dawod, IE; Brodmerkel, MN; Marklund, EG; Martin, A; Timneanu, N; Caleman, C
    Date
    2020-08-06
    Source Title
    Journal of Physical Chemistry Letters
    Publisher
    AMER CHEMICAL SOC
    University of Melbourne Author/s
    Martin, Andrew
    Affiliation
    School of Physics
    Metadata
    Show full item record
    Document Type
    Journal Article
    Citations
    Mandl, T., Ostlin, C., Dawod, I. E., Brodmerkel, M. N., Marklund, E. G., Martin, A., Timneanu, N. & Caleman, C. (2020). Structural Heterogeneity in Single Particle Imaging Using X-ray Lasers. JOURNAL OF PHYSICAL CHEMISTRY LETTERS, 11 (15), pp.6077-6083. https://doi.org/10.1021/acs.jpclett.0c01144.
    Access Status
    Open Access
    URI
    http://hdl.handle.net/11343/252468
    DOI
    10.1021/acs.jpclett.0c01144
    Abstract
    One of the challenges facing single particle imaging with ultrafast X-ray pulses is the structural heterogeneity of the sample to be imaged. For the method to succeed with weakly scattering samples, the diffracted images from a large number of individual proteins need to be averaged. The more the individual proteins differ in structure, the lower the achievable resolution in the final reconstructed image. We use molecular dynamics to simulate two globular proteins in vacuum, fully desolvated as well as with two different solvation layers, at various temperatures. We calculate the diffraction patterns based on the simulations and evaluate the noise in the averaged patterns arising from the structural differences and the surrounding water. Our simulations show that the presence of a minimal water coverage with an average 3 Å thickness will stabilize the protein, reducing the noise associated with structural heterogeneity, whereas additional water will generate more background noise.

    Export Reference in RIS Format     

    Endnote

    • Click on "Export Reference in RIS Format" and choose "open with... Endnote".

    Refworks

    • Click on "Export Reference in RIS Format". Login to Refworks, go to References => Import References


    Collections
    • Minerva Elements Records [45770]
    • School of Physics - Research Publications [937]
    Minerva AccessDepositing Your Work (for University of Melbourne Staff and Students)NewsFAQs

    BrowseCommunities & CollectionsBy Issue DateAuthorsTitlesSubjectsThis CollectionBy Issue DateAuthorsTitlesSubjects
    My AccountLoginRegister
    StatisticsMost Popular ItemsStatistics by CountryMost Popular Authors