title: Gas-phase structure of the E. coli OmpA dimer.
abstract: In this issue of Structure, Marcoux and colleagues use gas-phase collisional cross section (CCS) measured by ion-mobility mass spectrometry to analyze the CCS of oligomeric states of E. coli outer membrane OmpA. CCS of the dimer supports a model of paired periplasmic C-terminal domains projecting away from the transmembrane porins.
authors.affiliation: Pasarow Mass Spectrometry Laboratory, NPI-Semel Institute, David Geffen School of Medicine, UCLA, Los Angeles, CA 90095, USA. Electronic address: jpw@chem.ucla.edu.
authors.forename: Julian
authors.initials: J
authors.lastname: Whitelegge
mesh_terms: D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry*
chemical_list: D001425:Bacterial Outer Membrane Proteins; C078167:OMPA outer membrane proteins