AMPA receptor in an antagonist-bound state The AMPA receptor in an antagonist-bound closed state. The four colors delineate the four subunit chains in the receptor. Adapted from Meyerson et. al. 2014 Nature.

AMPA receptor in an antagonist-bound state

The AMPA receptor in an antagonist-bound closed state. The four colors delineate the four subunit chains in the receptor. Adapted from Meyerson et. al. 2014 Nature.

Conformations of the desensitized AMPA receptor Upon desensitization, the AMPA receptor ligand binding domain layer (orange) rearranges to have approximately four-fold in-plane symmetry. Also, the amino terminal domain layer (blue) is destabilized and becomes mobile. This mobility is captured in the three structures shown here. Adapted from Meyerson et. al. 2014 Nature.

Conformations of the desensitized AMPA receptor

Upon desensitization, the AMPA receptor ligand binding domain layer (orange) rearranges to have approximately four-fold in-plane symmetry. Also, the amino terminal domain layer (blue) is destabilized and becomes mobile. This mobility is captured in the three structures shown here. Adapted from Meyerson et. al. 2014 Nature.

Kainate receptor in a desensitized state The kainate type glutamate receptor in its desensitized state at a resolution of 7.6 Å. Adapted from Meyerson et. al. 2014 Nature.

Kainate receptor in a desensitized state

The kainate type glutamate receptor in its desensitized state at a resolution of 7.6 Å. Adapted from Meyerson et. al. 2014 Nature.

  The AMPA and kainate receptor gating cycles Models derived from structures of the three canonical functional states of AMPA and kainate glutamate receptors. The panel illustrates actions involved in transitioning between the different states. Illustration created by Donald Bliss of the National Library of Medicine. Adapted from Meyerson et. al. 2014 Nature.

 

The AMPA and kainate receptor gating cycles

Models derived from structures of the three canonical functional states of AMPA and kainate glutamate receptors. The panel illustrates actions involved in transitioning between the different states. Illustration created by Donald Bliss of the National Library of Medicine. Adapted from Meyerson et. al. 2014 Nature.

Preparation of SAM-grids and characterization of wettability The left and center columns illustrate the process of preparing cryo-EM grids modified with a self-assembled monolayer. The right hand column shows the grid wetability at each stage. Adapted from Meyerson et al. 2014 Sci Rep.

Preparation of SAM-grids and characterization of wettability

The left and center columns illustrate the process of preparing cryo-EM grids modified with a self-assembled monolayer. The right hand column shows the grid wetability at each stage. Adapted from Meyerson et al. 2014 Sci Rep.

Influenza virus with hemagglutinin molecules Renderings derived from cryo-electron tomograms of influenza virus particles, in combination with analysis from sub-tomogram classification and averaging. The image on the left shows the distribution of hemagglutinin proteins on the surface of the virus (green). The image on the right shows these same proteins, but some of them are bound by an antibody fragment (blue). The renderings were created by Amy Moran at the National Library of Medicine. Adapted from Harris and Meyerson et. al. 2013 Proc Natl Acad Sci USA.

Influenza virus with hemagglutinin molecules

Renderings derived from cryo-electron tomograms of influenza virus particles, in combination with analysis from sub-tomogram classification and averaging. The image on the left shows the distribution of hemagglutinin proteins on the surface of the virus (green). The image on the right shows these same proteins, but some of them are bound by an antibody fragment (blue). The renderings were created by Amy Moran at the National Library of Medicine. Adapted from Harris and Meyerson et. al. 2013 Proc Natl Acad Sci USA.

  HIV-1 viruses imaged by tomography Slices through cryo-electron tomograms of four different HIV-1 virus particles. The white arrows point to individual Envelope membrane protein spikes. Adapted from Meyerson et. al. 2013 Proc Natl Acad Sci USA.

 

HIV-1 viruses imaged by tomography

Slices through cryo-electron tomograms of four different HIV-1 virus particles. The white arrows point to individual Envelope membrane protein spikes. Adapted from Meyerson et. al. 2013 Proc Natl Acad Sci USA.

  Rendering of HIV-1 virus particle Rendering of a single HIV-1 virus segmented from a cryo-electron tomogram. The yellow, blue and red colors correspond to the virus core, membrane, and membrane spikes, respectively. Rendering created by Donald Bliss at the National Library of Medicine. Adapted from Meyerson et. al. 2013 J Vis Exp.

 

Rendering of HIV-1 virus particle

Rendering of a single HIV-1 virus segmented from a cryo-electron tomogram. The yellow, blue and red colors correspond to the virus core, membrane, and membrane spikes, respectively. Rendering created by Donald Bliss at the National Library of Medicine. Adapted from Meyerson et. al. 2013 J Vis Exp.

HIV-1 Envelope glycoprotein structures Shown on the left is the structure of the HIV-1 Envelope membrane glycoprotein without a binding partner. On the right, the Envelope protein is shown interacting with three copies of the A12 protein, a small domain antibody. The top row shows the structures derived by cryo-EM, and on the bottom these same structures are fitted with subunit structures from X-ray crystallography. Adapted from Meyerson et. al. 2013 Proc Natl Acad Sci USA.

HIV-1 Envelope glycoprotein structures

Shown on the left is the structure of the HIV-1 Envelope membrane glycoprotein without a binding partner. On the right, the Envelope protein is shown interacting with three copies of the A12 protein, a small domain antibody. The top row shows the structures derived by cryo-EM, and on the bottom these same structures are fitted with subunit structures from X-ray crystallography. Adapted from Meyerson et. al. 2013 Proc Natl Acad Sci USA.

HIV-1 gp120 trimer models In order for HIV-1 to infect a CD4+ T-cell, the Envelope protein undergoes dramatic rearrangements to accommodate binding with two partner proteins on the cell surface. These events culminate in fusion of the virus membrane with the cell, and infection. This collection of HIV-1 Envelope models show stages of this process, and were derived by fitting protein domains from crystallography into density maps derived from cryo-EM. Adapted from Meyerson et. al. 2013 Proc Natl Acad Sci USA.

HIV-1 gp120 trimer models

In order for HIV-1 to infect a CD4+ T-cell, the Envelope protein undergoes dramatic rearrangements to accommodate binding with two partner proteins on the cell surface. These events culminate in fusion of the virus membrane with the cell, and infection. This collection of HIV-1 Envelope models show stages of this process, and were derived by fitting protein domains from crystallography into density maps derived from cryo-EM. Adapted from Meyerson et. al. 2013 Proc Natl Acad Sci USA.