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A new electron diffraction technique called MicroED allows protein structures to be determined from three-dimensional microcrystals.

The antibody accessibility of the leptospiral surface protein, LigB, provides a guide for the rational design of improved recombinant chimeric vaccine antigens displayed on a single domain scaffold.

A conserved viral protein complex that promotes membrane wrapping of nascent herpesvirus particles shows structural similarity to cellular membrane-remodelling proteins, suggesting functional mimicry.

Internal dynamics play a crucial functional role in MarR (multiple antibiotic resistance repressor) proteins and their role reconciles the distinct allosteric mechanisms proposed previously.

The proteasomal deubiquitinase UCHL5/UCH37 uses a face distinct from the canonical ubiquitin binding site to engage K48-linked ubiquitin chains and catalyze chain debranching.

The crystal structure of Norrie Disease Protein in complex with the extracellular cysteine-rich domain of Frizzled4 receptor and sucrose octasulfate reveals binding sites for Frizzled4, low density lipoprotein receptor related protein 5/6, and proteoglycan.

Building on previous work (Shi et al., 2013), we have used MicroED to determine the structure of catalase at 3.2 Å resolution from a single crystal.

A large-scale phylogenetic inference of the ribonucleotide reductase family reveals a new distinct clade with implications on how nature adapted to environmental changes.

Structural and biophysical studies detail how Neisseria LbpB interacts with human lactoferrin for iron piracy and provides insight for how LbpB interacts with the antimicrobial peptide lactoferricin.

The structure of the trypanosome haptoglobin-haemoglobin receptor bound to its ligand reveals the molecular basis for ligand recognition in innate immunity and identifies molecular determinants that aid efficient uptake.