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To achieve industrially viable fabrication process for perovskite-based solar cells, every process step must be optimized for maximum throughput. We present a study of substituting laboratory-type UV-Ozone surface treatment with a high-throughput Corona treatment in a scalable perovskite solar cell fabrication process. It is observed that water contact angle measurements provide insufficient information to determine the necessary dose of Corona or UV-Ozone treatment, but the surface carbon signal measured by x-ray photoelectron spectroscopy accurately identifies when surface contamination has been completely removed. Furthermore, we observe highly accelerated de-contamination of ZnO surfaces by UV-Ozone treatment. The effect can be explained by photocatalytic O 2 − ion generation indicating that UV-Ozone treatment is also applicable in high-throughput processing. [ABSTRACT FROM AUTHOR]

TOM40 is the central component of the preprotein translocase of the mitochondrial outer membrane (TOM complex). We purified recombinant rat TOM40 (rTOM40), which was refolded in Brij35 after solubilization from inclusion bodies by guanidine HCl. rTOM40 (i) consisted of a 63% E-sheet structure and (ii) bound a matrix-targeted preprotein with high affinity and partially translocated it into the rTOM40 pore. This partial translocation was inhibited by stabilization of the mature domain of the precursor. (iii) rTOM40 bound preprotein initially through ionic interactions, followed by salt-resistant non-ionic interactions, and (iv) exhibited presequence-sensitive, cation-specific channel activity in reconstituted liposomes. Based on the domain structure of rTOM40 deduced by protease treatment, we purified the elastase-resistant and membrane-embedded C-terminal segment (rTOM40(ΔN165)) as a recombinant protein with 62% β-structure that exhibited properties comparable with those of full-size rTOM40. We concluded that the membrane-embedded C-terminal half of rTOM40 constitutes the preprotein recognition domain with an enriched β-structure, which forms the preprotein conducting pore containing a salt-sensitive cis-binding site and a salt-resistant trans-binding site. [ABSTRACT FROM AUTHOR]