Multimodal spectroscopy (smFRET, EPR, SAXS, and SANS) and integrative structural modeling reveal large-scale domain rearrangements in human guanylate binding protein 1 (hGBP1) that are driving forces for the formation of oligomers that enable its biological function in innate immune defense.

The integration of structural data from different imaging scales requires the development of standards and tools for representing the segmentation and transformation of data, and for the annotation of biological structures.

Integrative structural biology reveals a conformational equilibrium in the Box C/D methylation enzyme that regulates the extent of site-specific 2'-O-rRNA methylation in dependence of the RNA sequence.

The utilization of hydrogen/deuterium exchange mass spectrometry reveals dynamic insights and interactions driving liquid-liquid demixing of the chromosome passenger complex.

A summary of the current “state-of-the-field” of single-molecule FRET used for probing biomolecular structural dynamics.

Clustered and non-clustered protocadherins form antiparallel homodimers in which distinct regions of the extended interface demonstrate a division of labor between driving affinity and determining specificity.

Poxin enzymes are a diverse family of insect and viral 2′3′-cGAMP nucleases, which evolved from self-cleaving RNA virus accessory proteases.

Development of specific and high-affinity nanobodies to probe the structure of human acid sensing ion channel-1a and as binding modifiers of the toxins PcTx and MitTx1.

The 3D structure of the six-subunit complex and its polymeric assembly gives insights into cargo transport in cilia and how specific mutations in these genes lead to ciliopathy birth defects.