Coherent-Pulse 2D Crystallography Using a Free-Electron Laser X-Ray Source

Mancuso, Adrian P.; Schropp, Andreas; Reime, B.; Stadler, Lorenz-M.; Singer, Andrej; Gulden, J.; Streit-Nierobisch, S.; Gutt, Christian; Grübel, G.; Feldhaus, J.; Staier, Florian; Barth, R.; Rosenhahn, Axel; Grunze, M.; Nisius, Thomas; Wilhein, Thomas; Stickler, Daniel; Stillrich, Holger; Frömter, Robert; Oepen, Hans Peter; Martins, M.; Pfau, Bastian; Günther, C.; Könnecke, René; Eisebitt, Stefan; Faatz, B.; Guerassimova, N.; Honkavaara, K.; Kocharyan, Vitali; Treusch, R.; Saldin, E.L.; Schreiber, S.; Schneidmiller, E.A.; Yurkov, M.V.; Weckert, E.; Vartanyants, Ivan A.

doi:10.1103/physrevlett.102.035502

Cited by 49 publications

(40 citation statements)

References 24 publications

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“…2(c)). This is similar to observations in our previous experiments on coherent scattering from finite crystals [8,9,11,25]. We can see from this figure that we have sufficient detector resolution (more than five pixels per average fringe) to sample these speckles.…”

Section: Resultssupporting

confidence: 89%

Three-dimensional structure of a single colloidal crystal grain studied by coherent x-ray diffraction

et al. 2012

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Abstract:A coherent x-ray diffraction experiment was performed on an isolated colloidal crystal grain at the coherence beamline P10 at PETRA III. Using azimuthal rotation scans the three-dimensional (3D) scattered intensity from the sample in the far-field was measured. It includes several Bragg peaks as well as the coherent interference around these peaks. The analysis of the scattered intensity reveals the presence of plane defects in a single grain of the colloidal sample. We confirm these findings by model simulations.In these simulations we also analyze the experimental conditions required to phase the 3D diffraction pattern from a single colloidal grain. This approach has the potential to produce a high resolution image of the sample revealing its inner structure, with possible structural defects. Groot, and E. de Smit, "Scanning transmission x-ray microscopy as a novel tool to probe colloidal and photonic crystals," Small 7(6), 804-811 (2011 437-440 (2000). 16. J. Smajic, C. Hafner, and D. Erni, "Design and optimization of an achromatic photonic crystal bend," Opt. ©2012 Optical Society of AmericaExpress 11

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Section: Resultssupporting

confidence: 89%

Three-dimensional structure of a single colloidal crystal grain studied by coherent x-ray diffraction

et al. 2012

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“…This is similar to observations in our previous experiments on coherent scattering from large-period finite structures. 19 In addition to the allowed 220 Bragg peaks, we also observed much weaker forbidden peaks ͓1/3͑224͒ in our case͔. Their appearance is an indication of defects in the crystal.…”

Section: Resultsmentioning

confidence: 62%

“…For x-ray scattering methods one possible approach is to use large-period structures. 19 This is conveniently provided by nature in the form of colloidal crystals with a period in the range of a few hundred nanometers. Illuminating such samples with hard x-rays produces a diffraction pattern with many Bragg peaks mapped simultaneously on a twodimensional ͑2D͒ detector 20 and provides a convenient way to study the arrangement of colloidal particles.…”

Section: Introductionmentioning

confidence: 99%

Coherent x-ray imaging of defects in colloidal crystals

et al. 2010

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Coherent x-ray diffractive imaging ͑CXDI͒ was applied to reveal the structure of colloidal crystals. The colloidal sample was illuminated by a coherent x-ray beam through a 7 m pinhole aperture. The resulting diffraction patterns contain several Bragg peaks and an additional interference structure between the peaks due to the coherent illumination of a finite part of the sample. The inversion of these diffraction patterns reveals the arrangement of colloidal particles in a face-centered cubic ͑fcc͒ lattice as well as defects in the form of stacking faults in the ͑111͒ planes.

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“…The well-known phase problem is solved by using the oversampling method (29) in combination with the iterative algorithms (30)(31)(32)(33). Since its first experimental demonstration in 1999 (1), coherent diffraction microscopy has been applied to imaging a wide range of materials science and biological specimens such as nanoparticles, nanocrystals, biomaterials, cells, cellular organelles, viruses by using synchrotron radiation (2-21), high harmonic generation (22)(23)(24), soft X-ray laser sources (23,25), and free electron lasers (26)(27)(28). Until now, however, the radiation damage problem and the difficulty of acquiring high-quality 3D diffraction patterns from individual whole cells have prevented the successful high-resolution 3D imaging of biological cells by X-ray diffraction microscopy.…”

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confidence: 99%

Quantitative 3D imaging of whole, unstained cells by using X-ray diffraction microscopy

Jiang

Song

Chen

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

261

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Microscopy has greatly advanced our understanding of biology. Although significant progress has recently been made in optical microscopy to break the diffraction-limit barrier, reliance of such techniques on fluorescent labeling technologies prohibits quantitative 3D imaging of the entire contents of cells. Cryoelectron microscopy can image pleomorphic structures at a resolution of 3-5 nm, but is only applicable to thin or sectioned specimens. Here, we report quantitative 3D imaging of a whole, unstained cell at a resolution of 50-60 nm by X-ray diffraction microscopy. We identified the 3D morphology and structure of cellular organelles including cell wall, vacuole, endoplasmic reticulum, mitochondria, granules, nucleus, and nucleolus inside a yeast spore cell. Furthermore, we observed a 3D structure protruding from the reconstructed yeast spore, suggesting the spore germination process. Using cryogenic technologies, a 3D resolution of 5-10 nm should be achievable by X-ray diffraction microscopy. This work hence paves a way for quantitative 3D imaging of a wide range of biological specimens at nanometer-scale resolutions that are too thick for electron microscopy.coherent diffractive imaging | equally sloped tomography | lensless imaging | iterative phase-retrieval algorithms | oversampling A pplication of the long penetration depth of X-rays to the imaging of large, unstained biological specimens has long been recognized as a possible solution to the thickness restrictions of electron microscopy. Indeed, using sizable protein crystals, X-ray crystallography is currently the primary methodology used for determining the 3D structure of protein molecules at near-atomic or atomic resolution. However, many biological specimens such as whole cells, cellular organelles, some viruses, and many important protein molecules are difficult or impossible to crystallize and hence their structures are not accessible by crystallography. Overcoming these limitations requires the employment of different techniques. One promising approach currently under rapid development is coherent diffraction microscopy (also termed coherent diffractive imaging or lensless imaging) in which the coherent diffraction pattern of a noncrystalline specimen or a nanocrystal is measured and then directly phased to obtain an image (1-28). The well-known phase problem is solved by using the oversampling method (29) in combination with the iterative algorithms (30-33). Since its first experimental demonstration in 1999 (1), coherent diffraction microscopy has been applied to imaging a wide range of materials science and biological specimens such as nanoparticles, nanocrystals, biomaterials, cells, cellular organelles, viruses by using synchrotron radiation (2-21), high harmonic generation (22-24), soft X-ray laser sources (23, 25), and free electron lasers (26-28). Until now, however, the radiation damage problem and the difficulty of acquiring high-quality 3D diffraction patterns from individual whole cells have prevented the successful high-resolution ...

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Coherent-Pulse 2D Crystallography Using a Free-Electron Laser X-Ray Source

Cited by 49 publications

References 24 publications

Three-dimensional structure of a single colloidal crystal grain studied by coherent x-ray diffraction

Three-dimensional structure of a single colloidal crystal grain studied by coherent x-ray diffraction

Coherent x-ray imaging of defects in colloidal crystals

Quantitative 3D imaging of whole, unstained cells by using X-ray diffraction microscopy

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