Luke M. Oltrogge

The paper determines the structure of the DAB1 complex from Thermocrinis albus using cryo-EM, revealing how proton translocation couples to active-site remodeling for directional CO2 hydration.

This study investigates the trade-off between activity and specificity in adenine base editors using machine learning and high-throughput screening, finding that activity is the primary determinant of editing outcomes.

This paper uses cryoET to determine Rubisco polymerization constants in α-carboxysomes by converting tomography data into binding curves.

The paper introduces SABER, a method to efficiently map tolerated deletions in SaCas9, enabling the design of minimal CRISPRi effectors.

The paper maps the sequence-to-function relationship of rubisco by assaying single amino acid mutants in E. coli, identifying conserved positions and mutations that improve CO2 affinity.

This study identifies conserved and repetitive motifs in CsoS2 that drive α-carboxysome assembly and demonstrates in vitro reconstitution of carboxysomes.

The paper re-examines tradeoffs between Rubisco kinetic parameters using data from ~300 organisms, finding that most correlations are attenuated and only one tradeoff model remains.

The paper identifies a novel class of inorganic carbon transporters in chemoautotrophic bacteria through a genome-wide screen and characterizes their function as energy-coupled bicarbonate pumps.