3 research outputs found

    Role of Chloride in the Morphological Evolution of Organo-Lead Halide Perovskite Thin Films

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    A comprehensive morphological study was used to elucidate chloride’s role in CH<sub>3</sub>NH<sub>3</sub>PbI<sub>3–<i>x</i></sub>Cl<sub><i>x</i></sub> film evolution on a conducting polymer, PEDOT:PSS. Complex ion equilibria and aggregation in solution, as well as the role they play in nucleation, are found to ultimately be responsible for the unique morphological diversity observed in perovskite films grown in the presence of the chloride ion. An intermediate phase that is generated upon deposition and initial annealing templates continued self-assembly in the case of CH<sub>3</sub>NH<sub>3</sub>PbI<sub>3–<i>x</i></sub>Cl<sub><i>x</i></sub>. In the absence of chloride, the film growth of CH<sub>3</sub>NH<sub>3</sub>PbI<sub>3</sub> is directed by substrate interfacial energy. By employing the through-plane TEM analysis, we gain detailed insight into the unique crystallographic textures, grain structures, and elemental distributions across the breadth of films grown from precursor solutions with different chemistries. The lattice coherence seen in morphologies generated under the influence of chloride provides a physical rational for the enhancement in carrier diffusion length and lifetime

    Immobilization of Clostridium cellulolyticum d‑Psicose 3‑Epimerase on Artificial Oil Bodies

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    The rare sugar d-psicose possesses several fundamental biological functions. d-Psicose 3-epimerase from Clostridium cellulolyticum (CC-DPEase) has considerable potential for use in d-psicose production. In this study, CC-DPEase was fused to the N terminus of oleosin, a unique structural protein of seed oil bodies and was overexpressed in Escherichia coli as a CC-DPEase–oleosin fusion protein. After reconstitution into artificial oil bodies (AOBs), refolding, purification, and immobilization of the active CC-DPEase were simultaneously accomplished. Immobilization of CC-DPEase on AOB increased the optimal temperature but decreased the optimal pH of the enzyme activity. Furthermore, the AOB-immobilized CC-DPEase had a thermal stability and a bioconversion rate similar to those of the free-form enzyme and retained >50% of its initial activity after five cycles of enzyme use. Thus, AOB-immobilized CC-DPEase has potential application in the production of d-psicose at a lower cost than the free-form enzyme

    Additional file 1 of A radiomics-based deep learning approach to predict progression free-survival after tyrosine kinase inhibitor therapy in non-small cell lung cancer

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    Additional file 1: Table S1. The formulae for the calculation of primary radiomic features. Table S2. Grid search results of DeepSurv hyper-parameters. Table S3. Comparisons of clinical characteristics between training and test sets. Table S4. Characteristics of clinical laboratory test. Table S5. Identified features for the model training in each DeepSurv model. Figure S1. The architecture of applied DeepSurv model. Figure S2. Schematic diagram of predictive risk-of-progression period in DeepSurv model
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