Show simple item record

dc.contributor.authorMandl, T
dc.contributor.authorOstlin, C
dc.contributor.authorDawod, IE
dc.contributor.authorBrodmerkel, MN
dc.contributor.authorMarklund, EG
dc.contributor.authorMartin, A
dc.contributor.authorTimneanu, N
dc.contributor.authorCaleman, C
dc.date.accessioned2020-11-27T00:27:45Z
dc.date.available2020-11-27T00:27:45Z
dc.date.issued2020-08-06
dc.identifier.citationMandl, 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.
dc.identifier.issn1948-7185
dc.identifier.urihttp://hdl.handle.net/11343/252468
dc.description.abstractOne 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.
dc.languageEnglish
dc.publisherAMER CHEMICAL SOC
dc.rights.urihttps://creativecommons.org/licenses/by/4.0
dc.titleStructural Heterogeneity in Single Particle Imaging Using X-ray Lasers
dc.typeJournal Article
dc.identifier.doi10.1021/acs.jpclett.0c01144
melbourne.affiliation.departmentSchool of Physics
melbourne.source.titleJournal of Physical Chemistry Letters
melbourne.source.volume11
melbourne.source.issue15
melbourne.source.pages6077-6083
dc.rights.licensecc-by
melbourne.elementsid1455751
melbourne.contributor.authorMartin, Andrew
dc.identifier.eissn1948-7185
melbourne.accessrightsOpen Access


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record