Carolyn E. Mills

This study shows that altering charge on bacterial microcompartment shell proteins can control their self-assembly into tubular structures.

This paper introduces a standardized framework to quantify MS2 VLP reassembly yields and identifies key parameters affecting reassembly efficiency.

This study investigates how sequence variations in BMC-H proteins influence their self-assembly into different supramolecular structures using cell-free synthesis and microscopy.

The paper evaluates cofactor recycling and permeability in bacterial microcompartments using an in vitro assay and kinetic model of the Pdu system, showing benefits for pathway flux.

This study investigates the role of signal sequences in bacterial microcompartment (MCP) assembly, showing that structural protein signal sequences are critical for MCP formation and that their deletion causes defects similar to full gene knockout.

This study identifies PduB as the protein linking the 1,2-propanediol utilization MCP shell to its enzymatic core in Salmonella, showing shell and core assembly are separate processes.

GeneGrouper clusters gene clusters across taxa to identify functional or evolutionary patterns, revealing a novel pduN pseudogene in Salmonella enterica.

The paper shows that different imaging techniques produce varying apparent sizes and morphologies of bacterial microcompartments from Salmonella enterica serovar Typhimurium LT2, and provides guidelines for sample preparation.