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 6
Mutated residues within the crystal contact and their electron density. The B repeats of T336Y chains A, B and C are shown in dark blue, blue and cyan, respectively; the V333E variant is in green. The interrepeat region of the neighboring molecule is shown in grayscale. For the mutated residues, 2mF_o − DF_c electron-density maps are contoured at 1.0σ. Hydrogen bonds and the salt bridge involving the mutated side chains are shown as purple dashed lines. (a) T336Y chain A. (b) T336Y chain B. (c) T336Y chain C. (d) V333E; Glu333 is modeled in two conformations.

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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