Building on previous work (Froelich et al., 2014), we present the X-ray crystal structure of an active MCM hexamer, which suggests a mechanism for MCM regulation and demonstrates a key interaction between the major domains.

The crystal structure of a PfRh family protein from a malaria parasite has been solved and shows that PfRh5-which the parasite uses to invade human red blood cells-has a novel protein fold.

A combination of molecular dynamics simulations and X-ray diffraction data has been used to construct more realistic models of proteins and to provide new insights into their interactions with other proteins and biomolecules.

In the bacterial small multidrug transporter EmrE, sidechain rearrangements in the binding site accommodate structurally diverse substrates without major rearrangements of the protein backbone.

Polyunsaturated fatty acids enhance desensitization in pentameric ligand-gated ion channels.

Structural, functional, and genetic analyses reveal how kinesin-4 motor KLP-12 precisely modulates the curvature of the microtubule plus-end to inhibit the microtubule dynamics for achieving the proper length control of axons.

The structure of receptor-ligand complex reveals the ligand binding selectivity among different dopamine receptor subtypes and also shows how this ligand class inhibits receptor activity.

Substrate-induced structural changes in GtACR1 provide new insight into the chemical mechanism of natural light-gated anion conductance and facilitate its optimization for photoinhibition of neuron firing in optogenetics.

Crystal structures of an archaeal homologue of mammalian glutamate transporters in apo and ion-only bound outward- and inward-facing states reveal ion-coupled conformational changes supporting mechanisms of coupling, gating, and transport.

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.