Structure determination articles from across Nature Portfolio

The carbon fixation machinery α-carboxysome of the marine cyanobacterium Prochlorococcus is composed of an icosahedral-like proteinaceous shell that encapsulates the enzymes RuBisCO and carbonic anhydrase. Our cryo-EM structure reveals how thousands of protein components self-assemble into the α-carboxysome and characterizes the multivalent interactions by which the scaffolding protein CsoS2 crosslinks the shell with internal RuBisCO molecules.

Combining high-speed atomic force microscopy (AFM) with localization AFM and principal component analysis, the authors present six structures of a glutamate transporter and associate the conformational states to the molecule’s activity timeline.

Work by Klyshko and Kim et al. lays the foundation for simulating pump-probe experiments and demonstrates how the dynamic behaviour of proteins extends to the crystal environment, emphasizing the need for an ensemble view in understanding functional motions.

NARROW LEAF1 (NAL1) exerts a multifaceted influence on rice leaf morphology and yield. Recent crystal study proposed that histidine 233 (H233) is part of the catalytic triad. Here we report that H234 instead of H233 is a component of the catalytic triad alongside D291 and S385.

The cryo-EM structure shows us how thousands of protein components self-assemble into Prochlorococcus α-carboxysome. The scaffolding protein CsoS2 crosslinks the icosahedral-like shell and internal RuBisCOs, and determines the size of α-carboxysome.

It can be challenging to obtain meaningful and accurate structural information for air-sensitive proteins. This protocol describes the application of customized vacuum manifold and anaerobic chamber setups for the purification and cryo-electron microscopy analysis of air-sensitive nitrogenase enzymes.

How do cells put electrons to rest? Using a minimal pathway to get rid of excess metabolic electrons, diverse environmentally important microbes overcome large spatial, kinetic, and thermodynamic barriers in order to survive in extreme anoxic conditions.

The carbon fixation machinery α-carboxysome of the marine cyanobacterium Prochlorococcus is composed of an icosahedral-like proteinaceous shell that encapsulates the enzymes RuBisCO and carbonic anhydrase. Our cryo-EM structure reveals how thousands of protein components self-assemble into the α-carboxysome and characterizes the multivalent interactions by which the scaffolding protein CsoS2 crosslinks the shell with internal RuBisCO molecules.

The ATP-dependent chromatin remodeller DDM1 has a vital role in plant DNA methylation, influencing gene silencing and suppression of transposable elements. The structure of DDM1 in complex with nucleosome in different states of the ATP hydrolysis process reveals the molecular mechanism underlying chromatin remodelling by DDM1.

Developing therapeutic agents that target the peptidylarginine deiminase PAD4 requires better understanding of the function of the enzyme. Isozyme-selective antibodies that alter PAD4 activity have been identified recently, revealing unique modes of action.