Daniel P. Farrell

TL;DR: A structural model of the endogenously purified human canonical BAF complex bound to the nucleosome, generated using cryoelectron microscopy, cross-linking mass spectrometry, and homology modeling provides important biophysical foundations for understanding the mechanisms of BAFcomplex function in normal and disease states.

TL;DR: The 2019 Cryo-EM Model Challenge as discussed by the authors evaluated the quality of models that can be produced from Cryogenic EM maps using current modeling software, evaluating reproducibility of modeling results from different software developers and users and comparing performance of current metrics used for model evaluation, particularly Fit-to-Map metrics.

TL;DR: This work shows that the human BRM (hBRM) bromodomain (BRD) has moderate specificity for H3K14ac, and finds that both BRG1 and hBRM BRDs have DNA-binding activity, suggesting that association of theBRG1/h BRM BRD with nucleosomes plays a regulatory rather than targeting role in BAF activity.

TL;DR: This model provides the first detailed view of the machinery enabling ciliary exit and finds that BBSome subunits have a very high degree of interconnectivity, explaining the obligate nature of the complex.

TL;DR: In this article, the BRCA1/BARD1 RING heterodimer with the E2 enzyme UbcH5c bound to its cellular target, the nucleosome, along with biochemical data that explain how the complex selectively ubiquitylates lysines 125, 127 and 129 in the flexible C-terminal tail of H2A in a fully human system.