<i>In situ</i> monitoring of structure formation in the active layer of polymer solar cells during roll-to-roll coating

The active layer crystallization during roll-to-roll coating of organic solar cells is studied in situ. We developed an X-ray setup where the coater unit is an integrated part of the small angle X-ray scattering instrument, making it possible to control the coating process while recording scattering measurements in situ, enabling us to follow the crystal formation during drying. By varying the distance between the coating head and the point where the X-ray beam hits the film, we obtained measurements of 4 different stages of drying. For each of those stages, the scattering from as long a foil as possible is summed together, with the distance from coating head to scattering point kept constant. The results are average crystallographic properties for the active layer coated on a 30 m long foil. With this insight into the dynamics of crystallization in a roll-coated polymer film, we find that the formation of textured and untextured crystallites seems uncorrelated, and happens at widely different rates. Untextured P3HT crystallites form later in the drying process than expected which may explain previous studies speculating that untextured crystallization depends on concentration. Textured crystallites, however, begin forming much earlier and steadily increases as the film dries, showing a development similar to other in situ studies of these materials

Proteome Analysis of Pod and Seed Development in the Model Legume Lotus japonicus

Legume pods serve important functions during seed development and are themselves sources of food and feed. Compared to seeds, the metabolism and development of pods are not well-defined. The present characterization of pods from the model legume Lotus japonicus, together with the detailed analyses of the pod and seed proteomes in five developmental stages, paves the way for comparative pathway analysis and provides new metabolic information. Proteins were analyzed by two-dimensional gel electrophoresis and tandem-mass spectrometry. These analyses lead to the identification of 604 pod proteins and 965 seed proteins, including 263 proteins distinguishing the pod. The complete data set is publicly available at http://www.cbs.dtu.dk/cgi-bin/lotus/db.cgi, where spots in a reference map are linked to experimental data, such as matched peptides, quantification values, and gene accessions. Identified pod proteins represented enzymes from 85 different metabolic pathways, including storage globulins and a late embryogenesis abundant protein. In contrast to seed maturation, pod maturation was associated with decreasing total protein content, especially proteins involved in protein biosynthesis and photosynthesis. Proteins detected only in pods included three enzymes participating in the urea cycle and four in nitrogen and amino group metabolism, highlighting the importance of nitrogen metabolism during pod development. Additionally, five legume seed proteins previously unassigned in the glutamate metabolism pathway were identified