Structures of the yeast Sec14-like phosphatidylinositol transfer protein Sfh2 in complex with phosphatidylinositol and squalene reveal structural determinants for ligand recognition.

The crystal structure of human PTPRQ and the following kinetic data provide the explanation for its dephosphosphorylating activity towards phosphatidyl inositides.

Crystallization and diffraction analysis of a Ca²⁺-dependent PI-PLC from Streptomyces is reported. Optimization of crystals was completed using a drop-pinning technique and heavy-atom soaks to achieve high-quality diffraction to 1.23 Å.

The recombinant production and crystallization of the PitA adhesin from the Streptococcus oralis pilus island 2-encoded sortase-dependent pilus is described. Limited proteolysis of PitA and its complex with terbium crystallophore gave greatly improved X-ray diffraction to 2.16 Å resolution and a sufficiently strong anomalous signal for terbium SAD phasing, respectively.

Staphylococcus aureus SdrC forms a unique dimer through homophilic interactions, and a sandwich-like clamp at the C-terminus is formed by the two monomers in the stabilized SdrC dimer. Comparison with other Sdr proteins led to the proposal of a model for the confomational change of SdrC upon ligand binding.

Bond-cutting of Alq₃ by the doped K atoms occurs at high K concentration in a K-doped Alq₃ layer.

The synthesis, crystal structure and some spectroscopic details for (E)-1-(2,3-di­hydro­benzo[b][1,4]dioxin-6-yl)-3-(4-chloro­phen­yl)prop-2-en-1-one are presented.

The crystal structure of tert-butyl 3,6-di­iodo­carbazole-9-carboxyl­ate features inter­molecular π–π inter­actions, as well as both type I and type II inter­molecular II inter­actions.

The crystal structure of human inositol monophosphatase in complex with the substrate-based inhibitor L-690,330 is reported.

The packing of the title compound features C—HO hydrogen bonds, C—Fπ inter­actions, aromatic π–π stacking and short BrO contacts.