The crystal structure of an uncharacterized domain of P113 from Plasmodium falciparum

P113 is a membrane-anchored protein in Plasmodium falciparum that stabilizes the RH5 complex, facilitating erythrocyte invasion by interacting with the host receptor basigin. The helical-rich domain of P113 (residues 311–679) was crystallized, revealing a predominantly α-helical structure with two four-helix bundles and a disordered connecting region.

Structure of the Fab fragment of a humanized 5E5 antibody to a cancer-specific Tn-MUC1 epitope

The structure of the humanized Fab from murine monoclonal antibody 5E5 specific for tumor antigen Tn-MUC1 has been determined to 1.57 Å resolution. The humanization process has imposed changes in the framework regions of the Fv which may have affected the Vh–Vl interface.

Structures of α-galactosaminidases from the CAZy GH114 family and homologs defining a new GH191 family of glycosidases

Structural and functional analysis of a new fungal GH114 endo-α-1,4-galactosaminidase, along with homologs that establish a new GH191 family of glycoside hydrolases, are reported. In addition, various crystal pathologies led to the development of a new refinement procedure for disordered structures.

Unique double-helical packing of protein molecules in the crystal of potassium-independent L-asparaginase from common bean

The crystal structure of the potassium-independent L-asparaginase PvAIII, with a rare P2 space-group symmetry, shows an unusual pseudosymmetric 4₁-like double-helical packing with 32 protein chains in the asymmetric unit. The packing is determined by an extended intermolecular β-sheet, by incomplete degradation of the interdomain linker. and by intermolecular `hydrogen-bond linchpins' that connect adjacent protein chains together.