Since its invention at the beginning of the last century,
mass spectrometry (MS) has been considered an essen-
tial tool for chemists and physicists alike, primarily
being used to analyse small molecules and volatile com-
pounds. At the end of the 1980s, its utility broadened
dramatically, as its application to problems in biology
began in earnest. The ?rst reports on the MS of non-
covalent complexes appeared in the literature in the
early 1990s, with the initial studies focusing on
protein–ligand complexes quickly joined by those in
which protein–protein interactions were maintained

1
. Since those early days considerable improvements
in instrument technology and experimental method-
ology have dramatically increased the range of protein
assemblies amenable to MS analysis
2
. As a result,
20 years after the initial reports, assemblies as large
as intact viruses; of as many components as ribosomes;
as hydrophobic as membrane protein complexes; as het-
erogeneous as amyloidogenic oligomers; and as dynamic
as molecular chaperones have all been successfully
interrogated
3

7
. MS has therefore evolved to impact
a wide range of applications in structural biology.
In this historical perspective, we chart some of the
milestones in MS development as they pertain to the
study of non-covalent complexes, and

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