Author posts NanoScale

In a significant breakthrough, researchers at Ben-Gurion University’s Cryo-EM Unit, in collaboration with the Department of Life Sciences, have determined the near-atomic structure of a medically important membrane protein at 2.8 Å resolution. The structure sheds new light on the gating mechanism of a voltage-gated ion channel implicated in cardiac arrhythmias.

The cryo-EM data were collected on the unit’s Glacios 2 microscope over a three-day session, with over 4,000 micrograph movies acquired. Single-particle analysis was performed using RELION 4.0 and cryoSPARC, revealing distinct open and closed conformational states.

The findings have been submitted to Nature Structural & Molecular Biology and are currently available as a preprint on bioRxiv. The atomic model has been deposited in the RCSB Protein Data Bank (PDB).

Researchers using the Cryo-EM Unit’s tomography capabilities have published a landmark study revealing the three-dimensional cytoskeletal architecture inside intact Myxococcus xanthus bacterial cells. The work, published in eLife, used cryo-focused ion beam (cryo-FIB) milling combined with cryo-ET to visualize actin-like MreB filaments in their native cellular environment.

Sub-tomogram averaging of over 2,000 MreB filament segments yielded a resolution of approximately 8 Å, allowing the team to identify previously unknown lateral interactions between filaments that likely contribute to cell shape determination during biofilm formation.

This study represents the first cryo-ET dataset acquired entirely at the BGU facility and demonstrates the unit’s growing capabilities in whole-cell structural biology. The full tomographic dataset has been deposited in the EMDB and is publicly available for the community.

A multi-institutional collaboration led by researchers at Ben-Gurion University has determined the cryo-EM structure of an antibiotic-resistant bacterial ribosome at 3.1 Å resolution. The structure, published in Science, reveals precisely how a single point mutation in the 23S rRNA confers resistance to macrolide antibiotics, a clinically critical drug class.

The project involved research groups from BGU, Tel Aviv University, and the Hebrew University, with all cryo-EM data collected at the Ilse Katz Institute facility over a two-week campaign. More than 600,000 ribosome particles were picked and classified, ultimately yielding a consensus reconstruction with clearly resolved antibiotic binding site residues.

The structural insights from this work are already being used by the group to guide the rational design of next-generation antibiotics that can overcome the resistance mutation. A follow-up drug screening program is underway in collaboration with an Israeli pharmaceutical company.