Characterization of membrane-bound metalloproteins in the anaerobic ammonium-oxidizing bacterium "Candidatus Kuenenia stuttgartiensis" strain CSTR1.

Membrane-bound metalloproteins are the basis of biological energy conservation via respiratory processes, however, their biochemical characterization is difficult. Here, we followed a gel-based proteomics and metallomics approach to identify membrane-associated metalloproteins in the anaerobic ammonium-oxidizing "Candidatus Kuenenia stuttgartiensis" strain CSTR1. Membrane-associated protein complexes were separated by two dimensional Blue Native/SDS gel electrophoresis and subunits were identified by mass spectrometry; protein-bound metal ions were quantified from the gel by connecting either a desolvating nebulizer system or laser ablation to inductively coupled plasma triple quadrupole mass spectrometry (ICP-QqQ-MS).

Solvent influence on the surface morphology of P3HT thin films revealed by photoemission electron microscopy.

Only rigorous understanding of the relationship between the nanoscale morphology of organic thin films and the performance of the devices built from them will ultimately lead to design rules that can guide a structured development on the field of organic electronics. Despite great effort, unraveling the nanoscale structure of the films is still a challenge in itself. Here we demonstrate that photoemission electron microscopy can provide valuable insights into the chain orientation, domains size and grain boundary characteristics of P3HT films spun cast from different solvents at room as well as at elevated temperatures.