Cryoelectron microscopy of biological molecules is among the hottest growth areas in
biophysics and structural biology at present, and Frank is arguably the most distinguished …

Within cell membranes numerous protein assemblies reside. Among their many functions,
these assemblies regulate the movement of molecules between membranes, facilitate …

Advances in cryogenic electron microscopy (cryo-EM) enabled routine near-atomic structure
determination of membrane proteins, while nanodisc technology has provided a way to …

We used cryo-electron tomography in conjunction with single-particle averaging techniques
to study the structures of frozen-hydrated envelope glycoprotein (Env) complexes on intact …

A long-sought goal in structural biology has been the imaging of membrane proteins in their
membrane environments. This goal has been achieved with electron crystallography in …

We report the preparation and preliminary in vitro studies of nanocarriers termed
“buckysomes,” which are self-assembled, spherical nanostructures composed of the …

We report here the first three‐dimensional structure of the type 1 inositol 1, 4, 5‐
trisphosphate receptor (IP 3 R). From cryo‐electron microscopic images of purified receptors …

Apolipoprotein E (apoE), one of the major protein components of lipoproteins in the
peripheral and central nervous systems, regulates cholesterol metabolism through its …

Cryoelectronmicroscopy is a method for the imaging of macromolecules in the electron
microscope. It was originally developed to determine membrane protein structures from two …

For cryo-EM structural studies, we seek to image membrane proteins as single particles
embedded in proteoliposomes. One technical difficulty has been the low density of …