A major new national facility for electron microscopy, called EMPower, has been awarded to a consortium of Dutch universities and medical centers. EMPower aims to pave the way for major discoveries im...

SARS-CoV-2 variant booster vaccination broadens human B cell responses through the germinal center reaction.

Lövestam and Scheres present a cryo-EM structure of vault particles, found during tau filament extraction from progressive supranuclear palsy (PSP) brain tissue. They reveal a symmetry shift at the va...

Are you a creative postdoctoral-scientist keen to explore novel in-situ biology with cryogenic electron tomography? Do you have a background in imaging technologies and/or image processing?We are look...

In a groundbreaking advance that significantly deepens our understanding of viral replication machinery, researchers have unveiled high-resolution cryo-electron microscopy (cryo-EM) structures of the Nipah virus (NiV) polymerase complex. This detailed structural insight opens new avenues for the design of antiviral agents targeting a highly pathogenic zoonotic virus responsible for severe and often fatal human infections. Nipah virus, an emergent member of the Paramyxoviridae family, poses a persistent public health threat due to its zoonotic nature and the absence of approved therapeutics.

Vitellogenin (Vg) is the main yolk precursor lipoprotein in almost all egg-laying animals. In addition, along its evolutionary history, Vg has developed a range of new functions in different taxa. In the honey bee, Vg has functions related to immunity, antioxidant protection, social behavior and longevity. However, the molecular mechanisms underlying Vg functionalities are still poorly understood. Here, we report the cryo-EM structure of full-length honey bee Vg, one-step purified directly from hemolymph. The structure provides structural insights into the overall domain architecture, including the lipid binding cavity and the previously uncharacterized von Willebrand factor type D domain. A domain of unknown function has been identified as a C-terminal cystine knot domain based on structural homology. Information about post-translational modifications, cleavage products, metal and lipid binding allow an improved understanding of the mechanisms underlying the range of Vg functionalitie