Markus Mund

TL;DR: The data identify the supramolecular organization of Bax during apoptosis and support a molecular mechanism in which Bax fully or partially delineates pores of different sizes to permeabilize the mitochondrial outer membrane.

TL;DR: A real-time fitter for 3D single-molecule localization microscopy using experimental point spread functions (PSFs) that achieves minimal uncertainty in 3D on any microscope and is compatible with any PSF engineering approach is presented.

TL;DR: The stereotypic arrangement of proteins in the nuclear pore complex as in situ reference structures is exploited to characterize the performance of a variety of microscopy modalities, enabling 3D resolution calibration, assessment of labeling efficiency and precise molecular counting.

TL;DR: High-throughput superresolution microscopy is developed to reconstruct the nanoscale structural organization of 23 endocytic proteins from over 100,000 endocytosis sites in yeast and finds that proteins assemble by radially ordered recruitment according to function.

TL;DR: A fluorescence microscopy method is developed to track the average positions of yeast endocytic proteins in relation to each other with a time precision below 1 s and with a spatial precision of ∼10 nm, which shows how different coat proteins are distributed within the coat structure and how the assembly dynamics of N-BAR proteins relate to membrane shape changes.