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 24 June 2025

A high-resolution data set of fatty acid-binding protein structures. II: Crystallographic overview, ligand classes and binding pose

A high-quality set of 229 crystal structures of various isoforms of human and mouse fatty acid-binding proteins in apo and ligand-bound forms is presented. Many ligands have associated affinity data, which may help in the development of affinity- and pose-predicting algorithms.

Accepted 23 June 2025

Probabilistic single-particle cryo-EM ab initio 3D reconstruction in SIMPLE

We introduce a new approach to probabilistic multi-volume single-particle cryo-EM ab initio 3D reconstruction for simultaneous estimation of the relative particle 3D orientations and partitioning of the particles into groups with distinct structural states.

Accepted 13 June 2025

Structural dynamics of IDR interactions in human SFPQ and implications for liquid–liquid phase separation

SFPQ and NONO are DBHS-family proteins that are essential for transcriptional regulation and the assembly of paraspeckles, which are subnuclear structures built on the long noncoding RNA NEAT1. Through SAXS, SANS and XL-MS analyses, we reveal that the disordered regions of SFPQ surrounding its DBHS domain enable flexible interactions and that the full-length proteins are capable of dimer partner exchange, highlighting how these dynamics may contribute to phase separation and impact disease processes.

Accepted 13 June 2025

Crystal structure of coagulation factor XII N-terminal domains 1–5

Factor XII (FXII) is a plasma serine protease which becomes activated by interactions with polyanions such as polyphosphates from bacteria, with Zn2+ as a critical cofactor. The crystal structure of FXII domains 1–5, coupled with a second crystal structure of the isolated FnII domain in complex with Zn2+ ions, advances our understanding of FXII structure and ligand recognition.


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