Performance of the new biological small- and wide-angle X-ray scattering beamline 13A at the Taiwan Photon Source

Shih, Orion; Liao, K-F; Yeh, Y-Q; Su, C-J; Wang, C-A; Chang, JW; Wu, W-R; Liang, Cheng-Chih; Lin, Che-Ping; Lee, T-H; Chang, Chip-Hong; Chiang, L-C; Liu, D-G; Mh, Lee; Cy, Liu; Hsu, T-W; Mansel, Bradley W.; Ho, Meng-Chiao; Shu, C-Y; Lee, F; Yen, Eric; Lin, Tao; Jeng, U‐Ser

doi:10.1107/s1600576722001923

Cited by 29 publications

(14 citation statements)

References 34 publications

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“…To better elucidate the origin of the structural features observed in the blend films of the NFAs with PM6, simultaneous small- and wide-angle X-ray scattering (SAXS and WAXS; or SWAXS) was conducted at the TPS 13 A SWAXS end-station for revealing the solution conformations of the NFAs, PM6, and their complexes in chlorobenzene. , Sample concentrations in chlorobenzene are listed in Table S5. Solution SAXS model analysis is shown in Figure S10 and Tables S6 and 7, and WAXS peak analysis is shown in Figure S11 and Tables S8–9.…”

Section: Resultsmentioning

confidence: 99%

Unraveling the Structure–Property–Performance Relationships of Fused-Ring Nonfullerene Acceptors: Toward a C-Shaped ortho-Benzodipyrrole-Based Acceptor for Highly Efficient Organic Photovoltaics

Xue,

Lai,

et al. 2023

J. Am. Chem. Soc.

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The high-performance Y6-based nonfullerene acceptors (NFAs) feature a C-shaped A-DA'D-A-type molecular architecture with a central electron-deficient thiadiazole (Tz) A' unit. In this work, we designed and synthesized a new A-D-A-type NFA, termed CB16, having a C-shaped ortho-benzodipyrrole-based skeleton of Y6 but with the Tz unit eliminated. When processed with nonhalogenated xylene without using any additives, the binary PM6:CB16 devices display a remarkable power conversion efficiency (PCE) of 18.32% with a high open-circuit voltage (V oc ) of 0.92 V, surpassing the performance of the corresponding Y6-based devices. In contrast, similarly synthesized SB16, featuring an S-shaped parabenzodipyrrole-based skeleton, yields a low PCE of 0.15% due to the strong side-chain aggregation of SB16. The C-shaped A-D N B N D-A skeleton in CB16 and the Y6-series NFAs constitutes the essential structural foundation for achieving exceptional device performance. The central Tz moiety or other A' units can be employed to finely adjust intermolecular interactions. The single-crystal X-ray structure reveals that ortho-benzodipyrrole-embedded A-D N B N D-A plays an important role in the formation of a 3D elliptical network packing for efficient charge transport. Solution structures of the PM6:NFAs detected by small-and wide-angle X-ray scattering (SWAXS) indicate that removing the Tz unit in the C-shaped skeleton could reduce the self-packing of CB16, thereby enhancing the complexing and networking with PM6 in the spin-coating solution and the subsequent device film. Elucidating the structure−property−performance relationships of A-DA'D-A-type NFAs in this work paves the way for the future development of structurally simplified A-D-A-type NFAs.

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Section: Resultsmentioning

confidence: 99%

Unraveling the Structure–Property–Performance Relationships of Fused-Ring Nonfullerene Acceptors: Toward a C-Shaped ortho-Benzodipyrrole-Based Acceptor for Highly Efficient Organic Photovoltaics

Xue,

Lai,

et al. 2023

J. Am. Chem. Soc.

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“…Wide-angle X-ray scattering data for the sample before and after HER were measured with the TPS 13A BioSAXS beamline of NSRRC (Figure S7). 57 Imaging Characterizations. High-resolution TEM (HRTEM) and TEM−EDS images were taken using a JEOL JEM-2100 electron microscope operated at an accelerating voltage of 200 kV.…”

Section: Methodsmentioning

confidence: 99%

Arrayed Pt Single Atoms via Phosphotungstic Acids Intercalated in Silicate Nanochannels for Efficient Hydrogen Evolution Reactions

Chang,

Su,

Pao

et al. 2024

ACS Nano

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Single-atom catalysts, known for their high activity, have garnered significant interest. Currently, single-atom catalysts were prepared mainly on 2D substrates with random distribution. Here, we report a strategy for preparing arrayed single Pt (Pt 1 ) atoms, which are templated through coordination with phosphotungstic acids (PTA) intercalated inside hexagonally packed silicate nanochannels for a high single Pt-atom loading of ca. 3.0 wt %. X-ray absorption spectroscopy, high-angle annular dark-field scanning transmission electron microscopy, and energy-dispersive X-ray spectroscopy, in conjunction with the density-functional theory calculation, collectively indicate that the Pt single atoms are stabilized via a four-oxygen coordination on the PTA within the nanochannels' inner walls. The critical reduction in the Pt-adsorption energy to nearly the cohesive energy of Pt clustering is attributed to the interaction between PTA and the silicate substrate. Consequently, the transition from single-atom dispersion to clustering of Pt atoms can be controlled by adjusting the number density of PTA intercalated within the silicate nanochannels, specifically when the number ratio of Pt atoms to PTA changes from 3.7 to 18. The 3D organized Pt 1 −PTA pairs, facilitated by the arrayed silicate nanochannels, demonstrate high and stable efficiency with a hydrogen production rate of ca. 300 mmol/h/g Pt �approximately twice that of the best-reported Pt efficiency in polyoxometalate-based photocatalytic systems.

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“…The purified protein FtsBLQ with the unremoved His-tag at the concentration of 10 mg/ml in the buffer containing 20 mM HEPES pH7.5, 200 mM NaCl, 0.2% of Cymal-5 were used for SAXS measurement. SAXS data were collected at beamline TPS 13A BioSAXS of the National Synchrotron Radiation Research Center, Taiwan 51 , 52 . The SEC-SAXS system included a focused X-ray beam, in-vacuum Eiger X 9M and X 1M detectors coupled with an in-line HPLC unit (Agilent 1260 series), and a Bio SEC-3 silica-based column (pore size 300 Å, Agilent).…”

Section: Methodsmentioning

confidence: 99%

Structure of the heterotrimeric membrane protein complex FtsB-FtsL-FtsQ of the bacterial divisome

et al. 2023

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The synthesis of the cell-wall peptidoglycan during bacterial cell division is mediated by a multiprotein machine, called the divisome. The essential membrane protein complex of FtsB, FtsL and FtsQ (FtsBLQ) is at the heart of the divisome assembly cascade in Escherichia coli. This complex regulates the transglycosylation and transpeptidation activities of the FtsW-FtsI complex and PBP1b via coordination with FtsN, the trigger for the onset of constriction. Yet the underlying mechanism of FtsBLQ-mediated regulation is largely unknown. Here, we report the full-length structure of the heterotrimeric FtsBLQ complex, which reveals a V-shaped architecture in a tilted orientation. Such a conformation could be strengthened by the transmembrane and the coiled-coil domains of the FtsBL heterodimer, as well as an extended β-sheet of the C-terminal interaction site involving all three proteins. This trimeric structure may also facilitate interactions with other divisome proteins in an allosteric manner. These results lead us to propose a structure-based model that delineates the mechanism of the regulation of peptidoglycan synthases by the FtsBLQ complex.

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Performance of the new biological small- and wide-angle X-ray scattering beamline 13A at the Taiwan Photon Source

Cited by 29 publications

References 34 publications

Unraveling the Structure–Property–Performance Relationships of Fused-Ring Nonfullerene Acceptors: Toward a C-Shaped ortho-Benzodipyrrole-Based Acceptor for Highly Efficient Organic Photovoltaics

Unraveling the Structure–Property–Performance Relationships of Fused-Ring Nonfullerene Acceptors: Toward a C-Shaped ortho-Benzodipyrrole-Based Acceptor for Highly Efficient Organic Photovoltaics

Arrayed Pt Single Atoms via Phosphotungstic Acids Intercalated in Silicate Nanochannels for Efficient Hydrogen Evolution Reactions

Structure of the heterotrimeric membrane protein complex FtsB-FtsL-FtsQ of the bacterial divisome

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