CryoEM Workflow Acceleration with Feret Signatures.

Common challenges in cryogenic electron microscopy, such as orientation bias, conformational diversity, and 3D misclassification, complicate single particle analysis and lead to significant resource expenditure. We previously introduced an in silico method using the maximum Feret diameter distribution, the Feret signature, to characterize sample heterogeneity of disc-shaped samples. Here, we expanded the Feret signature methodology to identify preferred orientations of samples containing arbitrary shapes with only about 1000 particles required.

The mycoplasma surface proteins MIB and MIP promote the dissociation of the antibody-antigen interaction.

Mycoplasma immunoglobulin binding (MIB) and mycoplasma immunoglobulin protease (MIP) are surface proteins found in the majority of mycoplasma species, acting sequentially to capture antibodies and cleave off their V domains. Cryo-electron microscopy structures show how MIB and MIP bind to a Fab fragment in a "hug of death" mechanism. As a result, the orientation of the V and V domains is twisted out of alignment, disrupting the antigen binding site.

Study of the interaction between indole-based compounds and biologically relevant G-quadruplexes.

G-quadruplexes (G4s) are high-order secondary structures that modulate several key cell processes such as telomere function, gene expression and DNA replication. In the past years G4s have emerged as promising targets for drug development due to the discovery of small molecules which bind and stabilize these structures. In this work, we report the synthesis of indole-based compounds and the study of their interaction with the biological relevant G4s c-MYC and human telomeric repeat 22AG using several biophysical techniques.