A note on the appearance of PEG in macromolecular crystals

The use of polyethylene glycol in the crystallization of biological macromolecules and its appearance in the resulting crystals is discussed.

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

In its wild-type form, the flexible two-domain protein InlB₃₉₂ yielded poorly reproducible crystals that diffracted to low resolution. Single surface substitutions to tyrosine (T336Y) or glutamate (V333E) yielded well diffracting crystals, suggesting that surface properties, rather than interdomain flexibility, might be the primary impediment to crystallization of the wild type.

Crystal structure of Crocus vernus class IIIb chitinase: in silico ligand-binding studies and in vitro antifungal assay

This article describes the structural characterization of the class IIIb chitinase from Crocus vernus bulbs. Antifungal and chitinase assays have also been performed to evaluate the potential of the enzyme.

Crystal structure of Methanococcus jannaschii di­hydroorotase with substrate bound

We present the 1.87 Å resolution structure of M. jannaschii dihydroorotase complexed with the substrate carbamoyl aspartate at room temperature. Contrary to expectations, a flexible loop which is important in catalysis and closes upon substrate binding in order to stabilize the substrate and transition state is observed in both the loop-out and loop-in conformations, with the loop-out conformation having higher occupancy.

Potential 14-3-3 binding sites in sirtuins reveal extended phosphosite-recognition modes

Identification, binding measurements and structure determination of human sirtuin phosphopeptides in complex with human adapter protein 14-3-3σ reveal variations among tight binders and suggest extended binding modes.

Structure of the imine reductase from Ajellomyces dermatitidis in three crystal forms. Corrigendum

The article by Sharma et al. [(2023), Acta Cryst. F79, 224–230] is corrected.