The X-ray structure of the PaNhaP provides a unique view of substrate-ion binding and release in electroneutral sodium/proton antiporters.

An investigation into 8-oxodeoxguanosine bypass by archaeal DNA polymerases.

The inward-open and outward-open structures of MjNhaP1 explain the mechanism of electroneutral sodium-proton antiport across the cell membrane.

The genome of Thermovibrio ammonificans encodes ancestral pathways (e.g., hydrogen oxidation) and more recently acquired ones (e.g., nitrate reduction) and a hybrid pathway for CO₂ fixation.

Structural biology has elucidated the mechanism of a configuration-specific enzyme that decouples D-amino acids from the translational machinery and, therefore, is involved in the enforcement of homochirality during protein synthesis.

NusG enhances transcription elongation by stabilizing DNA base pairs immediately upstream of the RNA-DNA hybrid but does not measurably affect the nucleotide incorporation and the forward translocation by RNA polymerase.