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 5
Two geometries of the recurring crystal contact. Contact between the B repeat of one InlB₃₉₂ molecule (left; colored) and the interrepeat region of a neighboring molecule (right; grayscale). Side chains of the mutated residues (Glu333 and Tyr336) are shown as sticks. In the neighboring interrepeat region, Ser295 and Pro318 are shown as sticks to highlight aligned or shifted β-strand positions. (a) Overlay of T336Y chain A (dark blue) on chain B (blue) and their contacting neighbors (dark gray and gray). (b) Overlay of the V333E variant (green) on T336Y chain C (cyan) and their contacting neighbors (black and light gray). (c) Overlay of T336Y chains A (dark blue) on C (cyan) and their contacting neighbors (dark gray and light gray).

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