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The isolated 26S proteasome lid complex keeps the deubiquitinase in an inhibited state, which blocks peptides from accessing the active site (active site highlighted with green glow)
Atomic model determined from a cryo-EM structure of Rabbit TRPV2. Image by Mark Herzik
An interpretation of the proteasome degrading an ubiquitin-linked target substrate.
Bacteria wards off attacks from viruses by incorporating the invading RNA into a surveillance mechanism called Cascade
Identical assembly interfaces do not necessarily give rise to identical filament structures, as observed in this stylized comparison of Tubulin and TubZ subunits.
Peering down the barrel of a portal, the crystal structure of the bacteriophage P22 portal structure is docked into Jinghua Tang's subnanometer asymmetric reconstruction of the virion.
Visualizing ribosome biogenesis, Anke Mulder used time-resolved electron microscopy to monitor the assembly of the 30S subunit of the ribosome.
A flexible domain forms a cage around Drosophila A virus (DAV), as shown by the 8 Angstrom-resolution structure determined by cryoEM.
Mature bacteriophage P22 virions, with the tail machine fully assembled for infection. The tail machine is situated at a single pentameric vertex of the icosahedral capsid shell.
The architecture of an infection conduit. A subnanometer reconstruction of phage P22's genome packaging and delivery machine, called the tail machine, enabled a detailed description of its architecture.
A network of decoration proteins stabilize the bacteriophage lambda capsid shell. Trimers of the accessory protein gpD attach to the lambda capsid during viral maturation, stabilizing the delicate shell to cope with the pressures of DNA packaging
Welding together the bacteriophage lambda capsid. The N-terminal arm of the accessory protein gpD is flexible until it is integrated into the lambda shell, which in turn stabilizes the entire capsid. Image was made in collaboration with Graham Johnson.
DNA Packaging in phage lambda. Shown are the structures of the filled (left) and empty(right) capsids of bacteriophage labmda as determined by cryoEM, in collaboration with Alex Evilevitch.
A signal for headful packaging, the asymmetric cryoEM reconstruction of the bacteriophage P22 shows the manner in which the portal (shown in red) triggers the termination of DNA packaging. Image was made in collaboration with Graham Johnson.
The Appion pipeline. A conceptual rendition of streamlined processing of GroEL cryoEM data utilizing the Appion EM processing environment.
Assembly architecture of a viral terminase. The small subunit of the bacteriophage P22 terminase (shown in yellow) binds DNA and, as shown by the EM reconstruction, can accommodate its passage through a central channel. This work was performed in collaboration with Daniel Nemecek and George Thomas.