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.
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