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Updated: May 26, 2026

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
Published on: July 4, 2016
The polydispersity of αB-crystallin is rationalized by an interconverting polyhedral architecture
Andrew J Baldwin1, Hadi Lioe, Gillian R Hilton
1Department of Molecular Genetics, University of Toronto, 1 Kings College Circle, Toronto, ON M5S 1A8, Canada. ajb204@pound.med.utoronto.ca
Abstract:
We report structural models for the most abundant oligomers populated by the polydisperse molecular chaperone αB-crystallin. Subunit connectivity is determined by using restraints obtained from nuclear magnetic resonance spectroscopy and mass spectrometry measurements, enabling the construction of various oligomeric models. These candidate structures are filtered according to their correspondence with ion-mobility spectrometry data and cross-validated by using electron microscopy. The ensuing best-fit structures reveal the polyhedral architecture of αB-crystallin oligomers, and provide a rationale for their polydispersity and facile interconversion.
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