What are the advantages of the GSDIM method for your research?
In our research we try to understand how large multiprotein complexes, such as the nuclear pore complex (NPC), are built. Because of their size and complexity such molecular machines are beyond the scope of a single method and have long been a challenge for structural biology. Atomic-resolution methods such as X-ray crystallography or NMR require a purified specimen and are not suitable for very large assemblies. Although, electron microscopy allows the observation of large complexes in their native environment in the cell, it is often very difficult to assign the electron density to individual proteins. In fluorescence microscopy the identity of the protein is known and super-resolution (SR) now allows us to visualize details below the diffraction limit. When SR is combined with particle averaging, proteins' positions can be mapped to a subnanometer precision, a scale that makes light microscopy applicable to structural studies of large complexes. SR microscopy can therefore link different types of data and eventually help generate pseudo-atomic models of multiprotein assemblies. Additionally, a big advantage of especially