Jan Kosinski

TL;DR: This work combines cryo-electron tomography with mass spectrometry, biochemical analysis, perturbation experiments and structural modelling to generate the most comprehensive architectural model of the human nuclear pore complex to date.

TL;DR: This architectural map explains the vast majority of the electron density of the scaffold, and concludes that despite obvious differences in morphology and composition, the higher-order structure of the inner and outer rings is unexpectedly similar.

TL;DR: The accuracy and precision of mass spectrometry-based quantification is improved, enabling reliable protein half-life determination in several non-dividing cell types, illustrating that the approach allows investigating protein turnover and its implications in various cell types.

TL;DR: A new multi‐step protocol to predict the structures of all targets during CASP5, regardless of their potential category, using diverse fold‐recognition methods and the novelty of this approach is in the focus on “vertical” recombination of structure fragments, rather than “horizontal” sequence alignment typical for comparative modeling.

TL;DR: Cryo-electron microscopy structures of the Saccharomyces cerevisiae Pol III elongating complex and the apo Pol III enzyme in two different conformations are presented, providing novel insights into Pol III-specific transcription and the adaptation of Pol III towards its small transcriptional targets.