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

ABSTRACT: This case report describes single surface substitutions that improve the crystallizability and diffraction properties of a flexible two-domain protein. InlB₃₉₂ comprises the internalin domain and the B repeat of the Listeria monocytogenes invasion protein InlB. The InlB₃₉₂ wild type yielded very few poorly reproducible hits in crystallization screens and the crystals had a diffraction limit of worse than 3.0 Å. It seems reasonable to assume that this crystallization bottleneck is caused by interdomain flexibility, given that crystals of the isolated internalin domain or B repeat diffract to high resolution. A previously identified variant, T332E, showed improved crystallization and diffraction. Here, two additional InlB₃₉₂ variants are described with single

SUBMITTER: Geerds C 

PROVIDER: S-EPMC12809440 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature