A bacterial enzyme carries out a key step in carbon fixation which could provide a basis for engineering highly efficient CO2-fixing enzymes for bioenergy and bioproduct applications.

X-ray macromolecular crystallography reveals the structure and mode of interaction of the enzyme phenylalanyl-tRNA synthetase, which is integral to protein synthesis in a pathogenic bacterium.

Direct evidence reveals that hemicellulose forms pseudo-lignin aggregates during thermochemical pretreatment, which reduces enzyme accessibility and increases biomass recalcitrance.

Researchers have identified how iron-deficient plants optimize photosynthesis to protect themselves from absorbing too much light.

Macromolecular X-ray crystallography and small-angle X-ray scattering reveal surprising structural plasticity of RuBisCO, which underlies a rich phylogenetic diversity.

Enzyme-pseudoenzyme complexes involved in vitamin B6 synthesis in plants display variable stoichiometry.