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Coherent diffraction of single Rice Dwarf virus particles using hard X-rays at the Linac Coherent Light Source
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Molecular biophysics.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Molecular biophysics.
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2016 (English)In: Scientific Data, ISSN 1012-0602, E-ISSN 2052-4463, Vol. 3, 160064:1-12 p., 160064Article in journal (Refereed) Published
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Text
Place, publisher, year, edition, pages
2016. Vol. 3, 160064:1-12 p., 160064
National Category
Biophysics
Identifiers
URN: urn:nbn:se:uu:diva-300203DOI: 10.1038/sdata.2016.64ISI: 000390225700001OAI: oai:DiVA.org:uu-300203DiVA: diva2:951095
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eSSENCE
Available from: 2016-08-01 Created: 2016-08-05 Last updated: 2017-08-28Bibliographically approved
In thesis
1. Structural studies of small viruses using an X-ray Free Electron Laser
Open this publication in new window or tab >>Structural studies of small viruses using an X-ray Free Electron Laser
2016 (English)Licentiate thesis, comprehensive summary (Other academic)
Abstract [en]

X-ray crystallography has since its introduction been the most successful technique for solving protein structures. Viruses however, often possess structural components such as fibrils, tails and envelopes that make them difficult or impossible to crystallize. To explore virus structures and the structural changes they undergo during host entry and infection, instrumental developments are required. X-ray Free Electron Lasers posses some advantages compared to conventional synchrotron sources, which enable experiments that previously were impossible. The femtosecond pulses and peak brilliance that exceeds synchrotrons by 109 facilitate recording of diffraction from nano/microcrystals and single particles before radiation damage takes place. The challenges for XFELs to reach its true potential in structural biology are nevertheless still many. During the technical and computational developments, using well-characterized reference samples is advantageous. In this thesis, the Rice Dwarf virus and MS2 bacteriophage have been used for single particle imaging and crystallography experiments using XFELs. These viruses are two of the smallest biological samples so far studied as single particles using this technique and the crystallography data of MS2 presented might serve as basis for solving the first high-resolution genome structure.

Nanodiamonds, having a similar elemental composition as biological samples, could potentially serve as reference samples in XFEL studies. However, the biomedical field also has an interest in nanodiamonds, for drug delivery and as implant coating for example. Toxicity and biocompatibility is therefore a legitimate concern. Here, results from toxicity experiments of nanodiamonds on bacterial and zebrafish model organisms are presented.

Place, publisher, year, edition, pages
Uppsala: Uppsala Universitet, 2016. 30 p.
National Category
Structural Biology
Research subject
Physics with specialization in Biophysics
Identifiers
urn:nbn:se:uu:diva-303623 (URN)
Presentation
2016-10-13, C8:305, Biomedicinskt centrum, Husargatan 3, Uppsala, 10:15 (English)
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Available from: 2016-09-26 Created: 2016-09-21 Last updated: 2016-09-26

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Munke, AnnaAndreasson, JakobBielecki, JohanDaurer, Benedikt J.Hajdu, JanosHantke, Max F.Reddy, Hemanth K. N.Larsson, Daniel S. D.Maia, Filipe R. N. C.Mühlig, KerstinNettelblad, CarlOkamoto, Kentavan der Schot, GijsSeibert, M. MarvinSvenda, MartinTimneanu, NicusorWestphal, Daniel
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