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

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Figure 3
Interdomain flexibility between the internalin domain and the B repeat. The four crystallographically independent chains reported here are superposed on the internalin domain to highlight relative B-repeat motions. The InlB₃₉₂ V333E variant is shown in green and InlB₃₉₂ T336Y chains A, B and C are shown in dark blue, blue and cyan, respectively. N and C-termini are labeled. C^α atoms of the C-terminal residues are shown as spheres.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

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

https://doi.org/10.1107/S2053230X25010416

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