forthcoming articles

The following articles are a selection of those recently accepted for publication in Acta Crystallographica Section D: Structural Biology.

See also Forthcoming articles in all IUCr journals.

Accepted 31 March 2025

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

The crystal structure of 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 "H-bond linchpins" that connect adjacent protein chains together.

Accepted 28 March 2025

Robust error calibration for serial crystallography

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.

Accepted 27 March 2025

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.

Accepted 19 March 2025

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.


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