A brief history of macromolecular crystallography, illustrated by a family tree and its Nobel fruits

Abstract

As a contribution to the celebration of the year 2014, declared by the United Nations to be ‘The International Year of Crystallography’, the FEBS Journal is dedicating this issue to papers showcasing the intimate union between macromolecular crystallography and structural biology, both in historical perspective and in current research. Instead of a formal editorial piece, by way of introduction, this review discusses the most important, often iconic, achievements of crystallographers that led to major advances in our understanding of the structure and function of biological macromolecules. We identified at least 42 scientists who received Nobel Prizes in Physics, Chemistry or Medicine for their contributions that included the use of X‐rays or neutrons and crystallography, including 24 who made seminal discoveries in macromolecular sciences. Our spotlight is mostly, but not only, on the recipients of this most prestigious scientific honor, presented in approximately chronological order. As a summary of the review, we attempt to construct a genealogy tree of the principal lineages of protein crystallography, leading from the founding members to the present generation.

The Protein Data Bank archive as an open data resource

“…He went on to found the European Molecular Biology Laboratory. Kendrew, Perutz, and Hodgkin all received the Nobel Prize for their pioneering studies as did many other crystallographers [8]. In time, and perhaps not surprisingly, the structures of proteins began to emerge at a steady rate.…”

X-rays in the Cryo-Electron Microscopy Era: Structural Biology’s Dynamic Future

“…2 X-rays had been discovered by Wilhelm Röntgen less than two decades prior. In the wake of this discovery, the wave property of X-rays was still highly controversial.…”

Disruptive photon technologies for chemical dynamics

“…Macromolecular crystallography is a particularly important technique, and today almost 80% of all protein structures utilise synchrotron radiation at dedicated beamlines. This being the international year of crystallography there are many excellent recent reviews of this history [19][20][21] . The methodology of image synthesis has also been applied to noncrystalline samples, by using coherent X-ray beams to measure the continuous diffraction pattern [22][23][24] .…”