The structure of virus-like particles of the small RNA phage PRR1 bound to an RNA segment corresponding to a stem-loop that includes the start codon for the replicase gene has been solved and the binding was compared with the related, and better investigated, phage MS2.A.

The crystal structure of a synthetic consensus pentatricopeptide repeat protein displays helical disorder. The structure provides support for the utility of synthPPR as a backbone for designing bespoke RNA-binding proteins.

The crystal structures of the N-terminal tandem RRM domains of HuR are reported in RNA-free and RNA-bound forms.

Crystal structure determination of membrane proteins can be challenging. Here, the use of vanadium phasing as an alternative experimental phasing method is described.

The X-ray structures of viruses and viral proteins currently available are providing high-resolution snapshots of viral molecular machineries, expanding our vision of the virus world and giving crucial information on potential targets for future antiviral therapies.

Here, the recombinant ARE-binding region of HuR (residues 18-186) was crystallized in space group P2₁2₁2, with unit-cell parameters a = 41.2, b = 133.1, c = 31.4 Å.

virusMED (Virus Metal binding sites, Epitopes and Drug binding sites) is a rich internet application based on a database of atomic interactions around hotspots in 7041 experimentally determined viral protein structures.

The dimerization domain of splicing factor proline/glutamine-rich (SFPQ), an essential RNA-binding protein, has been crystallized in the C-centered orthorhombic space group C222₁ with one monomer in the asymmetric unit, and its structure has been determined and refined to 1.9 Å resolution. The crystal structure was analyzed and compared with the solution scattering data.

The 3.1 Å resolution single-particle cryo-electron microscopy structure of the RNA-bound Ebola virus nucleoprotein helical filament provides molecular details of protein–protein and protein–RNA interactions.

Crystal structures of the RecA-like domain 1 of Staphylococcus aureus CshA (SaCshA) and of its complex with AMP are reported; SaCshA shares a highly conserved ATP-binding mechanism with other DEAD-box RNA helicases.