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.

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.

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.

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.

We present a new error-calibration algorithm for reflection intensities in serial crystallography. We reformulate the mathematical basis of the problem and apply different levels of uncertainty to each observed lattice corresponding to its measurement accuracy. These uncertainties are more consistent with theoretical expectations than the Ev11 error-calibration algorithm previously implemented in cctbx.xfel.merge.