Carboxysomes, the carbon-fixation machinery of cyanobacteria, are equidistantly-positioned by dynamic gradients of the protein McdA on the nucleoid that emerge through interaction with a previously unidentified carboxysome factor, McdB.

Computational and theoretical models reveal mechanisms by which protein compartments assemble around enzymes and reagents to facilitate reactions in bacteria, allowing the identification of strategies for reengineering such compartments as customizable nanoreactors.

A bacterial CO₂ concentrating mechanism enables Escherichia coli to fix CO₂ from ambient air into biomass.

Systems level modeling of cyanobacterial mechanism for concentrating carbon dioxide shows optimal organization and enzymatic activity for enhanced carbon fixation.

The structures responsible for photosynthesis in bacteria use the nucleoid and two unique proteins as a scaffold to position themselves.

A mechanism for concentrating carbon dioxide has for the first time been successfully transferred into a species that lacks such a process.

In the PomX/Y/Z cell division regulatory system, PomX is a PomZ ATPase activating protein, a scaffold for PomX/Y/Z complex formation, and important for fission of the PomX/Y/Z complex during division.

The first 3D views of the native algal chloroplast provide new insights into thylakoid biogenesis, photosynthesis, and carbon fixation.

Nucleation, elasticity theory, and simulations were combined to construct a general phase diagram that elucidates the conditions for successful viral assembly and the key factors to prevent it.