Post-refinement methods enable the use of X-ray free electron lasers for biological crystallography of systems in which sample quantity is a limitation.
Structural and functional analyses show how the spliceosomal Prp3 protein concomitantly binds double- and single- stranded regions in U4/U6 di-snRNAs and serves to stabilize the U4/U6•U5 tri-snRNP for splicing.
The structure of the entire Mot1 Swi2/Snf2 protein uncovers an unexpected auto-inhibited resting state activated by substrate binding, and suggests a DNA pulling mechanism of TBP displacement.
The crystal structure of Thermus transcription activation complexes containing the transcriptional activator CarD reveals a new mechanism for the activation of transcription.
Single-molecule resolution of cAMP binding to the ligand binding domain of pacemaking channels in zero-mode waveguides reveals the dynamics of the distinct steps underlying both binding and isomerization of the binding domain.
The structure of the catalytic core of the N6-methyladenosine RNA methyltransferase complex METTL3-METTL14 reveals that METTL3 is the catalytic subunit, while METTL14 plays non-catalytic roles in substrate recognition and in maintaining complex integrity.