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The inner membrane-associated protein of 30 kDa (IM30) is essential in chloroplasts and cyanobacteria. The spatio-temporal cellular localization of the protein appears to be highly dynamic and triggered by internal as well as external stimuli, mainly light intensity. The soluble fraction of the protein is localized in the cyanobacterial cytoplasm or the chloroplast stroma, respectively. Additionally, the protein attaches to the thylakoid membrane as well as to the chloroplast inner envelope or the cyanobacterial cytoplasmic membrane, respectively, especially under conditions of membrane stress. IM30 is involved in thylakoid membrane biogenesis and/or maintenance, where it either stabilizes membranes and/or triggers membrane-fusion processes. These apparently contradicting functions have to be tightly controlled and separated spatiotemporally in chloroplasts and cyanobacteria. IM30's fusogenic activity depends on Mg

In organic electronics, local crystalline order is of critical importance for the charge transport. Grain boundaries between molecularly ordered domains are generally known to hamper or completely suppress charge transfer and detailed knowledge of the local electronic nature is critical for future minimization of such malicious defects. However, grain boundaries are typically hidden within the bulk film and consequently escape observation or investigation. Here, a minimal model system in form of monolayer-thin films with sub-nm roughness of a prototypical n-type organic semiconductor is presented. Since these films consist of large crystalline areas, the detailed energy landscape at single grain boundaries can be studied using Kelvin probe force microscopy. By controlling the charge-carrier density in the films electrostatically, the impact of the grain boundaries on charge transport in organic devices is modeled. First, two distinct types of grain boundaries are identified, namely energetic barriers and valleys, which can coexist within the same thin film. Their absolute height is found to be especially pronounced at charge-carrier densities below 10

The inner membrane-associated protein of 30 kDa (IM30) is essential in chloroplasts and cyanobacteria. The spatio-temporal cellular localization of the protein appears to be highly dynamic and triggered by internal as well as external stimuli, mainly light intensity. A soluble fraction of the protein is localized in the cyanobacterial cytoplasm or the chloroplast stroma, respectively. Additionally, the protein attaches to the thylakoid membrane as well as to the chloroplast inner envelope or the cyanobacterial cytoplasmic membrane, respectively, especially under conditions of membrane stress. IM30 is involved in thylakoid membrane biogenesis and/or maintenance, where it either stabilizes membranes and/or triggers membrane-fusion processes. These apparently contradicting processes have to be tightly controlled and separated spatiotemporally in chloroplasts and cyanobacteria. The latter process depends on Mg2+-binding to IM30; yet, it still is unclear how Mg2+-loaded IM30 interacts with membranes and promotes membrane fusion. Here we show that interaction of Mg2+ with IM30 results in increased binding of IM30 to native as well as model membranes. Via Atomic Force Microscopy in liquid, IM30-induced bilayer defects were observed in solid-supported bilayers in presence of Mg2+. The observed interaction of IM30 with membrane surfaces differs dramatically from previously observed membrane-stabilizing, carpet-like structures in the absence of Mg2+. Mg2+-induced alterations of the IM30 structure switches the IM30 activity from a membrane-stabilizing to a membrane-destabilizing function, a crucial step in membrane fusion.

Members of thephage shock protein A(PspA) family, including theinner membrane-associated protein of 30 kDa(IM30), are suggested to stabilize stressed cellular membranes. Furthermore, IM30 is essential in thylakoid membrane-containing chloroplasts and cyanobacteria, where it is involved in membrane biogenesis and/or remodeling. While it is well known that PspA and IM30 bind to membranes, the mechanism of membrane stabilization is still enigmatic. Here we report that ring-shaped IM30 super-complexes disassemble on membranes, resulting in formation of a membrane-protecting protein carpet. Upon ring dissociation, the C-terminal domain of IM30 unfolds, and the protomers self-assemble on membranes. IM30 assemblies at membranes have been observed beforein vivoand were associated to stress response in cyanobacteria and chloroplasts. These assemblies likely correspond to the here identified carpet structures. Our study defines the thus far enigmatic structural basis for the physiological function of IM30 and related proteins, including PspA, and highlights a hitherto unrecognized concept of membrane stabilization by intrinsically disordered proteins.

In this study we investigate the influence of the operation method in Kelvin probe force microscopy (KPFM) on the measured potential distribution. KPFM is widely used to map the nanoscale potential distribution in operating devices, e.g., in thin film transistors or on cross sections of functional solar cells. Quantitative surface potential measurements are crucial for understanding the operation principles of functional nanostructures in these electronic devices. Nevertheless, KPFM is prone to certain imaging artifacts, such as crosstalk from topography or stray electric fields. Here, we compare different amplitude modulation (AM) and frequency modulation (FM) KPFM methods on a reference structure consisting of an interdigitated electrode array. This structure mimics the sample geometry in device measurements, e.g., on thin film transistors or on solar cell cross sections. In particular, we investigate how quantitative different KPFM methods can measure a predefined externally applied voltage difference between the electrodes. We found that generally, FM-KPFM methods provide more quantitative results that are less affected by the presence of stray electric fields compared to AM-KPFM methods.

[Image: see text] We report that UV–ozone treatment of TiO(2) anatase thin films is an efficient method to increase the conductance through the film by more than 2 orders of magnitude. The increase in conductance is quantified via conductive scanning force microscopy on freshly annealed and UV–ozone-treated TiO(2) anatase thin films on fluorine-doped tin oxide substrates. The increased conductance of TiO(2) anatase thin films results in a 2% increase of the average power conversion efficiency (PCE) of methylammonium lead iodide-based perovskite solar cells. PCE values up to 19.5% for mesoporous solar cells are realized. The additional UV–ozone treatment results in a reduced number of oxygen vacancies at the surface, inferred from X-ray photoelectron spectroscopy. These oxygen vacancies at the surface act as charge carrier traps and hinder charge extraction from the adjacent material. Terahertz measurements indicate only minor changes of the bulk conductance, which underlines the importance of UV–ozone treatment to control surface-based defects.