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Träfflista för sökning "WFRF:(Kurta R. P.) "

Sökning: WFRF:(Kurta R. P.)

  • Resultat 1-7 av 7
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1.
  • Kurta, Ruslan P., et al. (författare)
  • Correlations in Scattered X-Ray Laser Pulses Reveal Nanoscale Structural Features of Viruses
  • 2017
  • Ingår i: Physical Review Letters. - : American Physical Society. - 0031-9007 .- 1079-7114. ; 119:15
  • Tidskriftsartikel (refereegranskat)abstract
    • We use extremely bright and ultrashort pulses from an x-ray free-electron laser (XFEL) to measure correlations in x rays scattered from individual bioparticles. This allows us to go beyond the traditional crystallography and single-particle imaging approaches for structure investigations. We employ angular correlations to recover the three-dimensional (3D) structure of nanoscale viruses from x-ray diffraction data measured at the Linac Coherent Light Source. Correlations provide us with a comprehensive structural fingerprint of a 3D virus, which we use both for model-based and ab initio structure recovery. The analyses reveal a clear indication that the structure of the viruses deviates from the expected perfect icosahedral symmetry. Our results anticipate exciting opportunities for XFEL studies of the structure and dynamics of nanoscale objects by means of angular correlations.
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2.
  • Reddy, Hemanth K. N., et al. (författare)
  • Coherent soft X-ray diffraction imaging of coliphage PR772 at the Linac coherent light source
  • 2017
  • Ingår i: Scientia Danica. Series H. Humanistica 4. - : Nature Publishing Group. - 1904-5506 .- 2052-4463. ; 4
  • Tidskriftsartikel (refereegranskat)abstract
    • 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.
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3.
  • Dzhigaev, D., et al. (författare)
  • Bragg coherent x-ray diffractive imaging of a single indium phosphide nanowire
  • 2016
  • Ingår i: Journal of Optics. - : IOP Publishing. - 2040-8978 .- 2040-8986. ; 18:6
  • Tidskriftsartikel (refereegranskat)abstract
    • Three-dimensional (3D) Bragg coherent x-ray diffractive imaging (CXDI) with a nanofocused beam was applied to quantitatively map the internal strain field of a single indium phosphide nanowire. The quantitative values of the strain were obtained by pre-characterization of the beam profile with transmission ptychography on a test sample. Our measurements revealed the 3D strain distribution in a region of 150 nm below the catalyst Au particle. We observed a slight gradient of the strain in the range of 0.6% along the [111] growth direction of the nanowire. We also determined the spatial resolution in our measurements to be about 10 nm in the direction perpendicular to the facets of the nanowire. The CXDI measurements were compared with the finite element method simulations and show a good agreement with our experimental results. The proposed approach can become an effective tool for in operando studies of the nanowires.
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4.
  • Ekeberg, Tomas, 1983-, et al. (författare)
  • Observation of a single protein by ultrafast X-ray diffraction
  • 2024
  • Ingår i: Light. - : Springer Nature. - 2095-5545 .- 2047-7538. ; 13:1
  • Tidskriftsartikel (refereegranskat)abstract
    • The idea of using ultrashort X-ray pulses to obtain images of single proteins frozen in time has fascinated and inspired many. It was one of the arguments for building X-ray free-electron lasers. According to theory, the extremely intense pulses provide sufficient signal to dispense with using crystals as an amplifier, and the ultrashort pulse duration permits capturing the diffraction data before the sample inevitably explodes. This was first demonstrated on biological samples a decade ago on the giant mimivirus. Since then, a large collaboration has been pushing the limit of the smallest sample that can be imaged. The ability to capture snapshots on the timescale of atomic vibrations, while keeping the sample at room temperature, may allow probing the entire conformational phase space of macromolecules. Here we show the first observation of an X-ray diffraction pattern from a single protein, that of Escherichia coli GroEL which at 14 nm in diameter is the smallest biological sample ever imaged by X-rays, and demonstrate that the concept of diffraction before destruction extends to single proteins. From the pattern, it is possible to determine the approximate orientation of the protein. Our experiment demonstrates the feasibility of ultrafast imaging of single proteins, opening the way to single-molecule time-resolved studies on the femtosecond timescale.
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5.
  • Rose, Max, et al. (författare)
  • Single-particle imaging without symmetry constraints at an X-ray free-electron laser
  • 2018
  • Ingår i: IUCrJ. - : INT UNION CRYSTALLOGRAPHY. - 2052-2525. ; 5, s. 727-736
  • Tidskriftsartikel (refereegranskat)abstract
    • The analysis of a single-particle imaging (SPI) experiment performed at the AMO beamline at LCLS as part of the SPI initiative is presented here. A workflow for the three-dimensional virus reconstruction of the PR772 bacteriophage from measured single-particle data is developed. It consists of several well defined steps including single-hit diffraction data classification, refined filtering of the classified data, reconstruction of three-dimensional scattered intensity from the experimental diffraction patterns by orientation determination and a final three-dimensional reconstruction of the virus electron density without symmetry constraints. The analysis developed here revealed and quantified nanoscale features of the PR772 virus measured in this experiment, with the obtained resolution better than 10 nm, with a clear indication that the structure was compressed in one direction and, as such, deviates from ideal icosahedral symmetry.
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6.
  • Shabalin, A. G., et al. (författare)
  • Revealing Three-Dimensional Structure of an Individual Colloidal Crystal Grain by Coherent X-Ray Diffractive Imaging
  • 2016
  • Ingår i: Physical Review Letters. - 0031-9007. ; 117:13
  • Tidskriftsartikel (refereegranskat)abstract
    • We present results of a coherent x-ray diffractive imaging experiment performed on a single colloidal crystal grain. The full three-dimensional (3D) reciprocal space map measured by an azimuthal rotational scan contained several orders of Bragg reflections together with the coherent interference signal between them. Applying the iterative phase retrieval approach, the 3D structure of the crystal grain was reconstructed and positions of individual colloidal particles were resolved. As a result, an exact stacking sequence of hexagonal close-packed layers including planar and linear defects were identified.
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7.
  • Delheusy, M., et al. (författare)
  • X-ray investigation of subsurface interstitial oxygen at Nb/oxide interfaces
  • 2008
  • Ingår i: Applied Physics Letters. - : AIP Publishing. - 0003-6951 .- 1077-3118. ; 92:10
  • Tidskriftsartikel (refereegranskat)abstract
    • We have investigated the dissolution of a natural oxide layer on a Nb(110) surface upon heating, combining x-ray reflectivity, grazing incidence diffuse scattering, and core-level spectroscopy. The natural oxide reduces after heating to 145 degrees C partially from Nb2O5 to NbO2, and an enrichment in subsurface interstitial oxygen by similar to 70% in a depth of 100 A is observed. After heating to 300 degrees C, the oxide reduces to NbO and the surplus subsurface oxygen gets dissolved into the bulk. Our approach can be applied for further investigation of the effect of subsurface interstitial oxygen on the performance of niobium rf cavities. (C) 2008 American Institute of Physics. (C) 2008 American Institute of Physics.
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  • Resultat 1-7 av 7

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