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Significance Chemical cross-linking coupled with mass spectrometry has recently emerged as a powerful method for providing medium-resolution spatial information for proteins that are too large or too flexible for crystallography or NMR. To date, crystal structures of only small segments of the highly flexible, conformationally dynamic spectrin family of proteins have been obtained. In this study we combined cross-link–derived spatial constraints with homology modeling to produce the first experimentally verified medium-resolution structures of wild-type spectrin closed dimers and tetramers. These structures coupled with the closed dimer structure of a very common spectrin mutation associated with hereditary hemolytic anemia provide mechanistic insights into how some mutations located large distances from the spectrin tetramerization site can destabilize red cell membranes.

Probing large conformational rearrangements in wild-type and mutant spectrin using structural mass spectrometry