I was hired as an intern at Nature Methods in 2005, fresh from my PhD in chemistry. The editors of Nature Methods were looking for an intern with chemistry expertise as they knew that many method advances important for biological research — the synthesis of chemical probes and dyes, the chemistry behind sequencing techniques, and the study of 3D protein structure, to name just a few — fundamentally stem from the chemistry field. My role was also somewhat strategic, as then Nature Publishing Group was making new forays into publishing chemistry research (Nature Chemical Biology and Nature Chemistry would soon launch as new journals). As I transitioned to a full-time editor later in 2005, I became the champion for what would become two major areas of the journal: proteomics and structural biology.

Cover design by Erin Dewalt.

In Nature Methods’ first 8 or so years, most of the papers we published in structural biology described advances in X-ray crystallography or NMR spectroscopy. But in late 2012 an interesting cryo-electron microscopy (cryo-EM) manuscript landed in my inbox. Submissions from this field, sometimes colloquially referred as ‘blobology’ owing to the low-resolution nature of 3D structures reconstructed using cryo-EM data, were few and far between. And the ones we did receive we mostly found to be too specialized to consider for peer review. This one, however, seemed like strong advance for cryo-EM. It proposed a new method using a single-electron-counting detector and an electron beam-induced motion-correction algorithm, and generated a 3.3 Å resolution structure of the Thermoplasma acidophilum 20S proteasome — still not quite as good as the best resolutions that could be achieved using X-ray crystallography, but a big leap for blobology.

I convinced my colleagues that we should peer-review the paper; grudgingly, they agreed to give it a chance. In all of my years as an editor have I rarely seen such glowing reviews. That paper is now recognized as one of the early works that ignited the ‘resolution revolution’ and the incredible transformation of cryo-EM into a mainstream technology for protein structure determination.

Unlike crystallography and NMR, which are largely limited to studying small, soluble proteins, cryo-EM is ideal for solving larger protein complexes and membrane proteins. The technology developments advancing cryo-EM thus helped to fill a major gap in the structural biology field. Scores of methodology and computational tool advances have continued to push this technique forward, many of which I am proud that Nature Methods has published. One of my favorite projects was highlighting cryo-EM as our Method of the Year pick in 2015. I continue to feel energized by this field and especially by new developments advancing the related technique of cryo-electron tomography, which allows the study of protein complexes in situ, in their native cellular environments.

Allison Doerr has been a manuscript editor at Nature Methods since 2005 and the Chief Editor since 2018.