Fig. 5
From: Simulations suggest a constrictive force is required for Gram-negative bacterial cell division
Effect of turgor pressure on the make-before-break mechanism. Two adjacent peptide crosslinks at a glycan break in a hoop are highlighted in cyan for visualization. a Without turgor pressure, the peptidoglycan (PG) was well ordered and the distance between the highlighted crosslinks was 4 nm. b Under turgor pressure, the cylinder expanded, peptides tilted, and the distance between the highlighted crosslinks increased to ~6.2 nm. θ depicts the tilting angle of a peptide crosslink. c Histogram of the tilting angles of all the peptide crosslinks (blue) and those connecting glycan termini (red). d An oblique view showing insertion of two new glycan strands in a make-before-break mechanism. When the new strand tips reach the first cyan-highlighted crosslink (indicated by the arrow head), they get ~0.4 nm ahead of their templates. e At the second cyan-highlighted crosslink (indicated by the double arrowhead), this small gain is offset by the additional 2.2 nm enlargement of the distance between the two crosslinks. f After the second highlighted crosslink, the strand tips fall behind their templates. g A break in the new glycan strands (indicated by the arrow) pulls the new strands forward, preventing them from falling behind their templates
