Single cell, fluorescent microscopy and mathematical modeling reveal how bacterial flagella dynamically assemble outside the cell.

A correlation between the periplasmic embellishment of the flagellar motor and its stator system type is described, motors with dual H+-dependent stator systems have one periplasmic ring formed by MotY.

The first high-resolution structure of a bacterial flagellar cap protein, FliD, reveals new insights into the assembly of bacterial flagella.

Bacteria reach swimming speeds of several hundred body lengths per second and change direction in less than 5 ms by using coordinated flagella bundle agitation.

Precise control of the bacterial flagellar motor determines bacterial cell dispersal and bacteria-surface interactions.

The length-dependent growth rate of bacterial flagellar filament is determined by the flagellin loading speed, loading strength and its diffusion process.

In situ structural analysis of bacterial flagellar motor in the Lyme disease spirochete reveals novel conformational change driven by proton motive force.

The swimming behavior of E. coli is surprisingly robust against the natural variations in the number of flagella per cell.

Both beneficial and pathogenic bacteria can use their sheathed flagella during host colonization as a novel toxin-/signal-delivery mechanism.

The corkscrew-like motility of Spirochete bacteria is enabled by a unique, asymmetrically constructed flagellum that wraps around the cell body within the periplasm.