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

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.

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.

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

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

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

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

In situ structures of the flagellar motors genetically docked in CCW and CW rotational states reveal major rearrangement that facilitates rotational switch in Vibrio alginolyticus..

Asymmetric forward and backward swimming speeds reveal that the rotational bias, and not reversal frequencies, is an appropriate measure of chemotaxis signaling in Helicobacter pylori..