A novel analytical workflow to quantitatively track motions of thousands of nucleosomes within chromatin fibers by high-speed atomic force microscopy.

A cluster of cofilin along an otherwise bare actin filament induces distinctively asymmetric cooperative conformational changes to the filament on either side of the cluster.

X-ray crystallographic and atomic force microscopic analyses reveal the tilted homodimer structure and unanticipated dynamic characteristics of canine distemper virus-hemagglutinin (CDV-H), providing insights into the molecular and dynamic processes of Morbillivirus for cell entry, effective immunizations, and vaccine/drug design.

During embryonic development, tissue stiffness, which provides an important signal to motile cells, changes locally within tens of minutes in a well-controlled manner.

Direct measurement of finely patterned mechanical properties in a native basement membrane demonstrate how force asymmetries arising from this extracellular matrix, rather than from cells, can precisely sculpt a tissue.

The isolation of the cell membrane of single cells coupled with AFM enables the study and identification of native membrane proteins in a membrane fragment.

The molecular mechanism that candidalysin uses to perforate membranes is unraveled, which opens the door to the rational design of inhibitors against candidiasis.

In triple-layered rotavirus particles, strong interaction between the external and middle layers provides high mechanical strength for protection tasks, while weaker interaction between the middle and inner layers favors transcription.

Atomic force microscopy reveals a floppy, dimeric, coiled coil Golgin structure that captures transport vesicles via splayed, N-terminal ends at the Golgi complex.

Electron and atomic force microscopy show how bacterial toxins bind to a host membrane and assemble into arcs and rings, before undergoing a dramatic, concerted conformational change to insert into the membrane.