Richard Henderson

Richard Henderson was born on July 19, 1945, in Edinburgh, Scotland. He is known for his groundbreaking work in the field of electron microscopy, which has significantly advanced our understanding of biological macromolecules. Henderson spent much of his career at the Laboratory of Molecular Biology in Cambridge, where he developed methods for the three-dimensional structure determination of proteins and contributed to the cryo-electron microscopy (cryo-EM) revolution.

In 1975, Richard Henderson and Nigel Unwin published a seminal paper in the Journal of Molecular Biology that reported the first structure of a membrane protein, bacteriorhodopsin, determined at atomic resolution. This pioneering work laid the foundation for the use of electron microscopy in structural biology, showing that it was possible to achieve high-resolution structures of proteins embedded in membranes, which were previously difficult to study.

By the 1990s, Richard Henderson was a leader in the development of three-dimensional electron microscopy techniques. His work focused on improving image processing methodologies to enhance the resolution and quality of 3D structures obtained through cryo-electron microscopy. This advancement revolutionized the field and allowed for the visualization of complex biomolecular structures, providing insight into biological processes at the molecular level.

In 1998, Richard Henderson achieved a significant milestone by determining the high-resolution structure of a 2D crystal of bacteriorhodopsin at a resolution finer than 3 Ångströms. This work was pivotal in demonstrating the potential of electron crystallography for determining membrane protein structures, inspiring further advancements and applications of cryo-electron microscopy in the study of biological macromolecules.

By 2013, Richard Henderson, along with other pioneers, significantly advanced the resolution of cryo-EM, pushing it to levels that enabled near-atomic resolution imaging of proteins. This breakthrough marked a transformative period in structural biology, allowing researchers to obtain detailed images of biomolecules, previously only possible through X-ray crystallography or NMR. These advancements opened new pathways for drug discovery and molecular biology research.

On October 4, 2017, Richard Henderson was awarded the Nobel Prize in Chemistry, alongside Jacques Dubochet and Joachim Frank, for their development of cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution. This prestigious recognition highlighted Henderson's pivotal contributions in revolutionizing structural biology, enabling scientists to observe biomolecular processes that were previously obscured by traditional methods.

In recognition of his extraordinary contributions to science, particularly in the field of electron microscopy, Richard Henderson was knighted by Queen Elizabeth II on February 2, 2018. This honor reflected Henderson's groundbreaking achievements in enhancing the capabilities of cryo-EM, which have provided profound insights into the structures of proteins and other macromolecules, and solidified the UK’s reputation as a leader in scientific research.

In May 2019, the release of the Falcon III direct electron detector was a significant upgrade in hardware technology supporting cryo-electron microscopy. Richard Henderson was significantly involved in the development and promotion of these new technologies, which expanded the potential for cryo-EM applications by greatly enhancing image quality and resolution, contributing to better structural data acquisition in research labs worldwide.

By the end of 2020, Richard Henderson continued to be at the forefront of advancements in cryo-electron microscopy, particularly in single particle analysis. His contributions have enhanced the accuracy and speed of data processing, further cementing cryo-EM as an essential tool in structural biology. This progress has made it feasible to determine structures of more complex and larger biomolecules at resolutions suitable for pharmaceutical and biochemical research.

On June 28, 2021, the UK opened its National Electron Cryo-Microscopy Centre, with Richard Henderson playing a key advisory role in its establishment. This facility aimed to provide state-of-the-art resources for scientists across the UK and internationally to access cryo-EM technology, fostering research collaborations and facilitating the visualization of cellular processes at atomic resolutions, thus driving innovations in medical and biological research.