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Twenty-five years ago, we obtained our first mass spectra of molecular chaperones in complex with protein ligands and entered a new field of gas-phase structural biology. It is perhaps now time to pause and reflect, and to ask how many of our initial structure predictions and models derived from mass spectrometry (MS) datasets were correct. With recent advances in structure determination, many of the most challenging complexes that we studied over the years have become tractable by other structural biology approaches enabling such comparisons to be made. Moreover, in the light of powerful new electron microscopy methods, what role is there now for MS? In considering these questions, I will give my personal view on progress and problems as well as my predictions for future directions.

Original publication




Journal article


Biochemical Society transactions

Publication Date





251 - 260


Department of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3QY, U.K.


Cell Membrane, Ribosomes, Thermus thermophilus, Bacterial Proteins, Chaperonin 60, Membrane Proteins, Molecular Chaperones, Microscopy, Electron, Protein Conformation, Models, Molecular, Time Factors, Molecular Motor Proteins, Mass Spectrometry, Adenosine Triphosphatases