Single mutations to tyrosine or glutamate improve the crystallizability and crystal diffraction properties of a flexible two-domain protein

Geerds, C.; Niemann, H.H.

doi:10.1107/S2053230X25010416

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

IUCr IT WDC

home archive editors for authors for readers submit subscribe open access

view article

Figure 4
A conserved crystal contact present in all InlB₃₉₂ structures. The coloring follows Fig. 2

(internalin domain, yellow/orange/red; B repeat, cyan). The four independent chains reported here are superposed on the B repeat (left molecule). All four form a crystal contact between strand β2 of the B repeat and the interrepeat region (red) of a neighboring internalin domain (right molecule). The dimeric arrangement shown is not C₂-symmetric. The B repeat of the right molecule forms the same contact with another neighbor.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 82| Part 1| January 2026| Pages 4-13

https://doi.org/10.1107/S2053230X25010416

Open

access

Follow Acta Cryst. F

Search IUCr Journals		doi		Advanced search
Author		volume	page