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Home > LMB News > The structure of bacteriorhodopsin 50 years on

The structure of bacteriorhodopsin 50 years on

Published on 4 August, 2025

Attendees of the symposium, shot from above.
Attendees of the recent symposium, celebrating the anniversary of the bacteriorhodopsin structure.

In 1975, Richard Henderson and Nigel Unwin published their landmark paper ‘Three-dimensional model of purple membrane obtained by electron microscopy’ in Nature. Describing the structure of the membrane protein bacteriorhodopsin to a resolution of 7 Å, the study was the first to produce a three-dimensional structure of a protein using electron microscopy and electron crystallography. This publication was the genesis of the ‘cryo-EM revolution’ that in the past 10 years has seen the technique become the gold-standard for structural studies of biological materials. To celebrate the legacy of this work, the LMB invited past and present colleagues and collaborators to discuss its ongoing impact at a symposium, ‘The structure of bacteriorhodopsin 50 years on: Electron cryomicroscopy and the dawn of membrane protein structural biology.’

LMB Group Leaders Chris Russo and Chris Tate, who helped organised the event, commented, “It was great to welcome so many familiar faces to the LMB and fantastic to see how generations of researchers have had their careers shaped by Richard and Nigel’s work.”

Black and white photo of Nigel Unwin and Richard Henderson
Nigel Unwin and Richard Henderson, 1991

The speakers, several of whom first learnt about the possible applications of cryo-EM under the tutelage of Richard and Nigel at the LMB, have gone on to work around the world, continuing to develop cryo-EM equipment and technology and applying the technique to increasingly complex biological systems. Many discussed how they have consistently adapted their research practices over the years to incorporate, and in some cases instigate, fast-moving advancements in the field of cryo-EM. Others, who have specialised in the study of membrane proteins, discussed how they had further illuminated the inner workings of bacteriorhodopsin, its many homologs and other proteins, and how these contribute to core biological processes.

Another source of interest during the event was a display of material prepared by Richard and Nigel, including notes, equipment and scan results the pair worked with in the 1970s. While gathering these items, Richard and Nigel also unearthed the schedule for the LMB’s annual symposium of research (often referred to as ‘Lab Talks’) from Thursday 4th October 1973. This event was the first occurrence, but by no means the last, that the duo shared the bill at a symposium, with Richard’s talk titled ‘Crystalline arrays of membrane proteins,’ followed just an hour later by Nigel who discussed ‘High resolution electron microscopy.’ Within two short years of speaking at this event, they had combined expertise and determined the structure of bacteriorhodopsin.

A uniting theme in the day’s talks was how decades of people’s research outputs have been buoyed by support from Nigel and Richard. Far beyond their initial paper 50 years ago, the pair have remained active in driving further developments in the field of structure determination. Several speakers discussed the willingness that both Nigel and Richard have displayed throughout the years to visit researchers at their labs or speak at meetings across the world, always eager to hear and discuss recent results or new ideas for projects. Many also shared recollections of writing to Richard and Nigel when faced with tricky problems in structural studies – Richard’s hand-written reply of ‘Never give up!’ in response to one missive succinctly summarised the pair’s approach to science.

Further references

Richard’s webpage
Nigel’s webpage
Three-dimensional model of purple membrane obtained by electron microscopy. Henderson, R. and Unwin, P. N. T. Nature

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