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 2
Structure of the InlB₃₉₂ V333E variant. Cartoon representation showing the internalin domain subdivided into the capping structure (yellow), leucine-rich repeats (orange) and the interrepeat region (red); the B repeat is cyan. Side chains at positions 333 and 336 are shown as sticks; in the V333E variant residue 336 is threonine (wild type) and Glu333 is modeled in two conformations. N- and C-termini are labeled.

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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