Coherent X-ray scattering beamline at port 9C of Pohang Light Source II

Yu, Chung-Jong; Lee, Hae Cheol; Kim, Chan; Cha, Wonsuk; Carnis, Jérôme; Kim, Yoonhee; Noh, Do Young; Kim, Hyun-Jung

doi:10.1107/s1600577513025629

Cited by 9 publications

(5 citation statements)

References 14 publications

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“…In case of weakly scattering objects, to obtain diffraction signal enough for the CDI reconstruction, one needs to increase incident photon flux by focusing [5,7,8] or increasing exposure. Typical flux of coherent x-ray beam on a sample from a third generation synchrotron is of order 10 9 photons s −1 [54]. Current efforts in developing synchrotron radiation sources of high flux and high degree of coherence such as diffraction limited ultimate rings [55,56] will be of great help for improving CDI resolution.…”

Section: Factors Determining Resolution In Coherent Diffraction Imagingmentioning

confidence: 99%

Enhancing resolution in coherent x-ray diffraction imaging

Noh

Kim

et al. 2016

J. Phys.: Condens. Matter

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Achieving a resolution near 1 nm is a critical issue in coherent x-ray diffraction imaging (CDI) for applications in materials and biology. Albeit with various advantages of CDI based on synchrotrons and newly developed x-ray free electron lasers, its applications would be limited without improving resolution well below 10 nm. Here, we review the issues and efforts in improving CDI resolution including various methods for resolution determination. Enhancing diffraction signal at large diffraction angles, with the aid of interference between neighboring strong scatterers or templates, is reviewed and discussed in terms of increasing signal-to-noise ratio. In addition, we discuss errors in image reconstruction algorithms-caused by the discreteness of the Fourier transformations involved-which degrade the spatial resolution, and suggest ways to correct them. We expect this review to be useful for applications of CDI in imaging weakly scattering soft matters using coherent x-ray sources including x-ray free electron lasers.

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Section: Factors Determining Resolution In Coherent Diffraction Imagingmentioning

confidence: 99%

Enhancing resolution in coherent x-ray diffraction imaging

Noh

Kim

et al. 2016

J. Phys.: Condens. Matter

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“…High-flux X-rays are provided by means of a 1.4 m-long hybrid-type in-vacuum undulator with a period of 20 mm (SFA, Korea). For the 3.0 GeV and 400 mA stored-beam-current PLS-II operating parameters, the undulator provides up to 2.95 kW of X-ray power (Yu et al, 2014). X-rays are monochromated (ÁE/E ' 10 À4 ) using a liquid-nitrogencooled silicon (111) double-crystal monochromator (Vactron, Korea) located 18 m from the X-ray source.…”

Section: Introductionmentioning

confidence: 99%

Hard X-ray nanotomography beamline 7C XNI at PLS-II

2014

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The synchrotron-based hard X-ray nanotomography beamline, named 7C X-ray Nano Imaging (XNI), was recently established at Pohang Light Source II. This beamline was constructed primarily for full-field imaging of the inner structures of biological and material samples. The beamline normally provides 46 nm resolution for still images and 100 nm resolution for tomographic images, with a 40 µm field of view. Additionally, for large-scale application, it is capable of a 110 µm field of view with an intermediate resolution.

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“…Diffraction data were collected at the Coherent X-ray Imaging (CXI) station at Pohang Accelerator Laboratory XFEL (Yu et al, 2014) [wavelength 1.278 A ˚, X-ray energy 9.7 keV, bandwidth 26 eV, beam size �3 � 4 mm (horizontal � vertical), 50 fs pulse width, 30 Hz repetition rate] at room temperature. Data were collected on a Rayonix MX225-HS CCD detector with 1440 � 1440 pixel resolution (4 � 4 binning, pixel size 156 mm) and a crystal-to-detector distance of 108 mm using serial femtosecond crystallography, as described previously (Lomb et al, 2011).…”

Section: Data Collection For Serial Femtosecond Crystallographymentioning

confidence: 99%

XFEL structure of carbonic anhydrase II: a comparative study of XFEL, NMR, X-ray and neutron structures

Hull,

Lee,

Kim

et al. 2024

Acta Cryst Sect D Struct Biol

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The combination of X-ray free-electron lasers (XFELs) with serial femtosecond crystallography represents cutting-edge technology in structural biology, allowing the study of enzyme reactions and dynamics in real time through the generation of `molecular movies'. This technology combines short and precise high-energy X-ray exposure to a stream of protein microcrystals. Here, the XFEL structure of carbonic anhydrase II, a ubiquitous enzyme responsible for the interconversion of CO2 and bicarbonate, is reported, and is compared with previously reported NMR and synchrotron X-ray and neutron single-crystal structures.

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Coherent X-ray scattering beamline at port 9C of Pohang Light Source II

Cited by 9 publications

References 14 publications

Enhancing resolution in coherent x-ray diffraction imaging

Enhancing resolution in coherent x-ray diffraction imaging

Hard X-ray nanotomography beamline 7C XNI at PLS-II

XFEL structure of carbonic anhydrase II: a comparative study of XFEL, NMR, X-ray and neutron structures

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