Joaquin Ortega

TL;DR: It is shown that recombinant, polyhistidine-tagged (his- tagged) Pfs25 can be mixed at the time of immunization with pre-formed liposomes containing cobalt porphyrin–phospholipid, resulting in spontaneous nanoliposome antigen particleization (SNAP).

TL;DR: Structural and biochemical analysis of a ribosome particle depleted of L16 indicate that L16 binding is necessary for the stimulation of RbgA GTPase activity and, in turn, release of this co-factor, and for conversion of the intermediate to a complete 50S subunit.

TL;DR: It is shown that rapid conversion of recombinant RBD into particulate form via admixing with liposomes containing cobalt‐porphyrin‐phospholipid (CoPoP) potently enhances the functional antibody response.

TL;DR: This structure represents the first visualization of the conformational changes induced by an assembly factor in a bacterial subunit intermediate and shows that upon interaction of RbgA with the 45SRbgA particle, Histidine 9 positions itself near the nucleotide potentially acting as the catalytic residue with minimal rearrangements.

TL;DR: The discussions were largely focused on supporting single-particle methods for cryoEM and topics included: user access, assessing projects, workflow, sample handling, microscopy, data management and processing, and user training.