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BETA
Seibert, Marvin
Alternative names
Publications (10 of 62) Show all publications
Reddy, H. K. N., Yoon, C. H., Aquila, A., Awel, S., Ayyer, K., Barty, A., . . . Xavier Paulraj, L. (2017). Coherent soft X-ray diffraction imaging of Coliphage PR772 at the Linac coherent light source. Scientific Data, 4, Article ID 170079.
Open this publication in new window or tab >>Coherent soft X-ray diffraction imaging of Coliphage PR772 at the Linac coherent light source
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2017 (English)In: Scientific Data, E-ISSN 2052-4463, Vol. 4, article id 170079Article in journal (Refereed) Published
Abstract [en]

Single-particle diffraction from X-ray Free Electron Lasers offers the potential for molecular structure determination without the need for crystallization. In an effort to further develop the technique, we present a dataset of coherent soft X-ray diffraction images of Coliphage PR772 virus, collected at the Atomic Molecular Optics (AMO) beamline with pnCCD detectors in the LAMP instrument at the Linac Coherent Light Source. The diameter of PR772 ranges from 65-70 nm, which is considerably smaller than the previously reported similar to 600 nm diameter Mimivirus. This reflects continued progress in XFEL-based single-particle imaging towards the single molecular imaging regime. The data set contains significantly more single particle hits than collected in previous experiments, enabling the development of improved statistical analysis, reconstruction algorithms, and quantitative metrics to determine resolution and self-consistency.

National Category
Biophysics
Identifiers
urn:nbn:se:uu:diva-328536 (URN)10.1038/sdata.2017.79 (DOI)000404232100001 ()28654088 (PubMedID)
Projects
eSSENCE
Funder
Swedish Research CouncilKnut and Alice Wallenberg FoundationEU, European Research CouncilThe Swedish Foundation for International Cooperation in Research and Higher Education (STINT)
Available from: 2017-06-27 Created: 2017-08-25 Last updated: 2017-11-29Bibliographically approved
Daurer, B. J., Okamoto, K., Bielecki, J., Maia, F. R. .., Mühlig, K., Seibert, M. M., . . . Larsson, D. S. D. (2017). Experimental strategies for imaging bioparticles with femtosecond hard X-ray pulses. IUCrJ, 4(3), 251-262
Open this publication in new window or tab >>Experimental strategies for imaging bioparticles with femtosecond hard X-ray pulses
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2017 (English)In: IUCrJ, ISSN 0972-6918, E-ISSN 2052-2525, Vol. 4, no 3, p. 251-262Article in journal (Refereed) Published
Abstract [en]

This study explores the capabilities of the Coherent X-ray Imaging Instrument at the Linac Coherent Light Source to image small biological samples. The weak signal from small samples puts a significant demand on the experiment. Aerosolized Omono River virus particles of similar to 40 nm in diameter were injected into the submicrometre X-ray focus at a reduced pressure. Diffraction patterns were recorded on two area detectors. The statistical nature of the measurements from many individual particles provided information about the intensity profile of the X-ray beam, phase variations in the wavefront and the size distribution of the injected particles. The results point to a wider than expected size distribution (from similar to 35 to similar to 300 nm in diameter). This is likely to be owing to nonvolatile contaminants from larger droplets during aerosolization and droplet evaporation. The results suggest that the concentration of nonvolatile contaminants and the ratio between the volumes of the initial droplet and the sample particles is critical in such studies. The maximum beam intensity in the focus was found to be 1.9 * 10(12) photons per mu m(2) per pulse. The full-width of the focus at half-maximum was estimated to be 500 nm (assuming 20% beamline transmission), and this width is larger than expected. Under these conditions, the diffraction signal from a sample-sized particle remained above the average background to a resolution of 4.25 nm. The results suggest that reducing the size of the initial droplets during aerosolization is necessary to bring small particles into the scope of detailed structural studies with X-ray lasers.

Keyword
X-ray diffraction, free-electron laser, flash X-ray imaging, diffraction before destruction, virus, Omono River virus, OmRV
National Category
Chemical Sciences Biophysics
Identifiers
urn:nbn:se:uu:diva-323439 (URN)10.1107/S2052252517003591 (DOI)000400460500008 ()28512572 (PubMedID)
Projects
eSSENCE
Funder
Swedish Research CouncilKnut and Alice Wallenberg FoundationEU, European Research CouncilSwedish Foundation for Strategic Research The Swedish Foundation for International Cooperation in Research and Higher Education (STINT)Helge Ax:son Johnsons stiftelse
Available from: 2017-11-14 Created: 2017-11-14 Last updated: 2018-01-02Bibliographically approved
Popp, D., Loh, N. D., Zorgati, H., Ghoshdastider, U., Liow, L. T., Ivanova, M. I., . . . Robinson, R. C. (2017). Flow-aligned, single-shot fiber diffraction using a femtosecond X-ray free-electron laser. Paper presented at International Symposium on Now in Actin, DEC, 2016, Nagoya Univ, Nagoya, JAPAN. CYTOSKELETON, 74(12), 472-481
Open this publication in new window or tab >>Flow-aligned, single-shot fiber diffraction using a femtosecond X-ray free-electron laser
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2017 (English)In: CYTOSKELETON, ISSN 1949-3584, Vol. 74, no 12, p. 472-481Article in journal (Refereed) Published
Abstract [en]

A major goal for X-ray free-electron laser (XFEL) based science is to elucidate structures of biological molecules without the need for crystals. Filament systems may provide some of the first single macromolecular structures elucidated by XFEL radiation, since they contain one-dimensional translational symmetry and thereby occupy the diffraction intensity region between the extremes of crystals and single molecules. Here, we demonstrate flow alignment of as few as 100 filaments (Escherichia coli pili, F-actin, and amyloid fibrils), which when intersected by femtosecond X-ray pulses result in diffraction patterns similar to those obtained from classical fiber diffraction studies. We also determine that F-actin can be flow-aligned to a disorientation of approximately 5 degrees. Using this XFEL-based technique, we determine that gelsolin amyloids are comprised of stacked -strands running perpendicular to the filament axis, and that a range of order from fibrillar to crystalline is discernable for individual -synuclein amyloids.

Place, publisher, year, edition, pages
WILEY, 2017
Keyword
fiber diffraction, filament systems, XFEL
National Category
Cell Biology
Identifiers
urn:nbn:se:uu:diva-340293 (URN)10.1002/cm.21378 (DOI)000417746200005 ()28574190 (PubMedID)
Conference
International Symposium on Now in Actin, DEC, 2016, Nagoya Univ, Nagoya, JAPAN
Funder
Knut and Alice Wallenberg FoundationSwedish Research CouncilThe Swedish Foundation for International Cooperation in Research and Higher Education (STINT)
Available from: 2018-01-29 Created: 2018-01-29 Last updated: 2018-01-29Bibliographically approved
Ryan, R. A., Williams, S., Martin, A. V., Dilanian, R. A., Darmanin, C., Putkunz, C. T., . . . Abbey, B. (2017). Measurements of Long-range Electronic Correlations During Femtosecond Diffraction Experiments Performed on Nanocrystals of Buckminsterfullerene. Journal of Visualized Experiments (126), Article ID e56296.
Open this publication in new window or tab >>Measurements of Long-range Electronic Correlations During Femtosecond Diffraction Experiments Performed on Nanocrystals of Buckminsterfullerene
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2017 (English)In: Journal of Visualized Experiments, ISSN 1940-087X, E-ISSN 1940-087X, no 126, article id e56296Article in journal (Refereed) Published
Abstract [en]

The precise details of the interaction of intense X-ray pulses with matter are a topic of intense interest to researchers attempting to interpret the results of femtosecond X-ray free electron laser (XFEL) experiments. An increasing number of experimental observations have shown that although nuclear motion can be negligible, given a short enough incident pulse duration, electronic motion cannot be ignored. The current and widely accepted models assume that although electrons undergo dynamics driven by interaction with the pulse, their motion could largely be considered 'random'. This would then allow the supposedly incoherent contribution from the electronic motion to be treated as a continuous background signal and thus ignored. The original aim of our experiment was to precisely measure the change in intensity of individual Bragg peaks, due to X-ray induced electronic damage in a model system, crystalline C-60. Contrary to this expectation, we observed that at the highest X-ray intensities, the electron dynamics in C-60 were in fact highly correlated, and over sufficiently long distances that the positions of the Bragg reflections are significantly altered. This paper describes in detail the methods and protocols used for these experiments, which were conducted both at the Linac Coherent Light Source (LCLS) and the Australian Synchrotron (AS) as well as the crystallographic approaches used to analyse the data.

Keyword
Chemistry, Issue 126, Nanocrystallography, Femtosecond X-ray Diffraction, Correlated Electron Dynamics, X-ray Free Electron Lasers, Linac Coherent Light Source, Buckminsterfullerene
National Category
Biophysics
Identifiers
urn:nbn:se:uu:diva-343144 (URN)10.3791/56296 (DOI)000415369500095 ()
Available from: 2018-02-26 Created: 2018-02-26 Last updated: 2018-02-26Bibliographically approved
Hantke, M. F., Hasse, D., Ekeberg, T., John, K., Svenda, M., Loh, D., . . . Maia, F. R. .. (2016). A data set from flash X-ray imaging of carboxysomes. Scientific Data, 3, Article ID 160061.
Open this publication in new window or tab >>A data set from flash X-ray imaging of carboxysomes
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2016 (English)In: Scientific Data, E-ISSN 2052-4463, Vol. 3, article id 160061Article in journal (Refereed) Published
Abstract [en]

Ultra-intense femtosecond X-ray pulses from X-ray lasers permit structural studies on single particles and biomolecules without crystals. We present a large data set on inherently heterogeneous, polyhedral carboxysome particles. Carboxysomes are cell organelles that vary in size and facilitate up to 40% of Earth’s carbon fixation by cyanobacteria and certain proteobacteria. Variation in size hinders crystallization. Carboxysomes appear icosahedral in the electron microscope. A protein shell encapsulates a large number of Rubisco molecules in paracrystalline arrays inside the organelle. We used carboxysomes with a mean diameter of 115±26 nm from Halothiobacillus neapolitanus. A new aerosol sample-injector allowed us to record 70,000 low-noise diffraction patterns in 12 min. Every diffraction pattern is a unique structure measurement and high-throughput imaging allows sampling the space of structural variability. The different structures can be separated and phased directly from the diffraction data and open a way for accurate, high-throughput studies on structures and structural heterogeneity in biology and elsewhere.

National Category
Biophysics
Identifiers
urn:nbn:se:uu:diva-300202 (URN)10.1038/sdata.2016.61 (DOI)000390225400006 ()
Note

Data Descriptor

Available from: 2016-08-05 Created: 2016-08-05 Last updated: 2017-11-28Bibliographically approved
Munke, A., Andreasson, J., Aquila, A., Awel, S., Ayyer, K., Barty, A., . . . Zook, J. (2016). Coherent diffraction of single Rice Dwarf virus particles using hard X-rays at the Linac Coherent Light Source. Scientific Data, 3, 160064:1-12, Article ID 160064.
Open this publication in new window or tab >>Coherent diffraction of single Rice Dwarf virus particles using hard X-rays at the Linac Coherent Light Source
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2016 (English)In: Scientific Data, E-ISSN 2052-4463, Vol. 3, p. 160064:1-12, article id 160064Article in journal (Refereed) Published
National Category
Biophysics
Identifiers
urn:nbn:se:uu:diva-300203 (URN)10.1038/sdata.2016.64 (DOI)000390225700001 ()
Projects
eSSENCE
Available from: 2016-08-01 Created: 2016-08-05 Last updated: 2017-11-28Bibliographically approved
van der Schot, G., Svenda, M., Maia, F. R. .., Hantke, M. F., DePonte, D. P., Seibert, M. M., . . . Ekeberg, T. (2016). Open data set of live cyanobacterial cells imaged using an X-ray laser. Scientific Data, 3, Article ID 160058.
Open this publication in new window or tab >>Open data set of live cyanobacterial cells imaged using an X-ray laser
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2016 (English)In: Scientific Data, E-ISSN 2052-4463, Vol. 3, article id 160058Article in journal (Refereed) Published
Abstract [en]

Structural studies on living cells by conventional methods are limited to low resolution because radiation damage kills cells long before the necessary dose for high resolution can be delivered. X-ray free-electron lasers circumvent this problem by outrunning key damage processes with an ultra-short and extremely bright coherent X-ray pulse. Diffraction-before-destruction experiments provide high-resolution data from cells that are alive when the femtosecond X-ray pulse traverses the sample. This paper presents two data sets from micron-sized cyanobacteria obtained at the Linac Coherent Light Source, containing a total of 199,000 diffraction patterns. Utilizing this type of diffraction data will require the development of new analysis methods and algorithms for studying structure and structural variability in large populations of cells and to create abstract models. Such studies will allow us to understand living cells and populations of cells in new ways. New X-ray lasers, like the European XFEL, will produce billions of pulses per day, and could open new areas in structural sciences.

National Category
Biophysics
Identifiers
urn:nbn:se:uu:diva-300201 (URN)10.1038/sdata.2016.58 (DOI)000390225400003 ()
Note

Data Descriptor

Available from: 2016-08-05 Created: 2016-08-05 Last updated: 2017-11-28Bibliographically approved
Ekeberg, T., Svenda, M., Seibert, M. M., Abergel, C., Maia, F. R. .., Seltzer, V., . . . Hajdu, J. (2016). Single-shot diffraction data from the Mimivirus particle using an X-ray free-electron laser. Scientific Data, 3, Article ID UNSP 160060.
Open this publication in new window or tab >>Single-shot diffraction data from the Mimivirus particle using an X-ray free-electron laser
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2016 (English)In: Scientific Data, E-ISSN 2052-4463, Vol. 3, article id UNSP 160060Article in journal (Refereed) Published
Abstract [en]

Free-electron lasers (FEL) hold the potential to revolutionize structural biology by producing X-ray pules short enough to outrun radiation damage, thus allowing imaging of biological samples without the limitation from radiation damage. Thus, a major part of the scientific case for the first FELs was three-dimensional (3D) reconstruction of non-crystalline biological objects. In a recent publication we demonstrated the first 3D reconstruction of a biological object from an X-ray FEL using this technique. The sample was the giant Mimivirus, which is one of the largest known viruses with a diameter of 450 nm. Here we present the dataset used for this successful reconstruction. Data-analysis methods for single-particle imaging at FELs are undergoing heavy development but data collection relies on very limited time available through a highly competitive proposal process. This dataset provides experimental data to the entire community and could boost algorithm development and provide a benchmark dataset for new algorithms.

National Category
Atom and Molecular Physics and Optics
Identifiers
urn:nbn:se:uu:diva-314814 (URN)10.1038/sdata.2016.60 (DOI)000390225400005 ()
Funder
Swedish Research CouncilKnut and Alice Wallenberg FoundationEU, European Research CouncilStiftelsen Olle Engkvist Byggmästare
Available from: 2017-02-07 Created: 2017-02-06 Last updated: 2017-11-29Bibliographically approved
van der Schot, G., Svenda, M., Maia, F. R. N., Hantke, M., DePonte, D. P., Seibert, M. M., . . . Ekeberg, T. (2015). Imaging single cells in a beam of live cyanobacteria with an X-ray laser. Nature Communications, 6, Article ID 5704.
Open this publication in new window or tab >>Imaging single cells in a beam of live cyanobacteria with an X-ray laser
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2015 (English)In: Nature Communications, ISSN 2041-1723, E-ISSN 2041-1723, Vol. 6, article id 5704Article in journal (Refereed) Published
Abstract [en]

There exists a conspicuous gap of knowledge about the organization of life at mesoscopic levels. Ultra-fast coherent diffractive imaging with X-ray free-electron lasers can probe structures at the relevant length scales and may reach sub-nanometer resolution on micron-sized living cells. Here we show that we can introduce a beam of aerosolised cyanobacteria into the focus of the Linac Coherent Light Source and record diffraction patterns from individual living cells at very low noise levels and at high hit ratios. We obtain two-dimensional projection images directly from the diffraction patterns, and present the results as synthetic X-ray Nomarski images calculated from the complex-valued reconstructions. We further demonstrate that it is possible to record diffraction data to nanometer resolution on live cells with X-ray lasers. Extension to sub-nanometer resolution is within reach, although improvements in pulse parameters and X-ray area detectors will be necessary to unlock this potential.

National Category
Structural Biology
Identifiers
urn:nbn:se:uu:diva-245040 (URN)10.1038/ncomms6704 (DOI)000350034400002 ()25669616 (PubMedID)
Available from: 2015-02-24 Created: 2015-02-24 Last updated: 2017-12-04Bibliographically approved
Ekeberg, T., Svenda, M., Abergel, C., Maia, F. R. N., Seltzer, V., Claverie, J.-M., . . . Hajdu, J. (2015). Three-dimensional reconstruction of the giant mimivirus particle with an X-ray free-electron laser. Physical Review Letters, 114(9), 098102:1-6, Article ID 098102.
Open this publication in new window or tab >>Three-dimensional reconstruction of the giant mimivirus particle with an X-ray free-electron laser
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2015 (English)In: Physical Review Letters, ISSN 0031-9007, E-ISSN 1079-7114, Vol. 114, no 9, p. 098102:1-6, article id 098102Article in journal (Refereed) Published
National Category
Biophysics
Identifiers
urn:nbn:se:uu:diva-246129 (URN)10.1103/PhysRevLett.114.098102 (DOI)000351000300010 ()25793853 (PubMedID)
Available from: 2015-03-02 Created: 2015-03-02 Last updated: 2017-08-28Bibliographically approved
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