M. Elizabeth Stroupe

The paper identifies critical amino acid residues in the N-terminal domain of SiRFP that mediate octameric assembly, revealing their role in stabilizing the enzyme's structure.

The paper analyzes the structure of Mycoplasma penetrans MetRS, revealing it as an asymmetric dimer with N-terminal ancillary domains and a partially resolved MetRS domain.

The paper determines the 2.78 Å resolution cryo-EM structure of Escherichia coli SiR, revealing the minimal interface for diflavin reductase binding and distinguishing between hemoprotein and ferredoxin partner interactions.

The paper introduces SPOT-RASTR, a cryo-EM technique using lipid nanotubes to overcome air-water interface and preferred orientation issues, enabling automated data collection and near-atomic resolution.