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Biography

Dr Briony Yorke is a lecturer in physical chemistry at the University of Leeds. Briony completed her MChem in the school of chemistry at the University of Leeds, where she worked on methods for time-resolved optical spectroscopy under the supervision of Prof. Godfrey Beddard. She then moved across the University of Leeds campus to the Astbury centre for structural molecular biology to complete her PhD where she applied time-resolved methods to X-ray crystallographic methods. Her supervisory team was led by Professor Arwen Pearson, Professor Michael Webb (University of Leeds) and Dr Robin Owen (Diamond Light Source, UK). In the final year of her PhD she moved with Professor Pearson to the centre for ultrafast imaging in the experimental physics department at the University of Hamburg. Here she worked as a post-doctoral fellow before being awarded a Sir Henry Wellcome Post-Doctoral Fellowship supervised by Professor Paul Raithby (University of Bath) and Professor Arwen Pearson (centre for ultrafast imaging, Hamburg). 

In 2020, Briony started a lectureship in structural biology at the University of Bradford, supported by the Academy of Medical Science springboard award. She then moved to the University of Leeds in 2023 where she is a member of the Astbury Centre for structural biology. Briony works closely with researchers at international synchrotron facilities including Diamond Light Source and EMBL@PetraIII where she develops new methods for time-resolved experiments. She is the vice chair of the biological structures group of the British Crystallographic Society and sits on the executive committee and equity, diversity and inclusion team of CCP4.

Collaboration is key, we are all continually learning and a positive culture allows us to grow together.

Briony Yorke

Q&A

Can you tell us more about your work?

As biological systems carry out the processes essential for life, they rely on molecules that move, change shape, and interact with one another on extremely fast timescales. To truly understand how these processes work we must expand our three-dimensional structural models to include information about how these molecules move.
 
Proteins act as the molecular machinery of the cell, controlling processes ranging from energy conversion to signalling. However, many of the most important steps in their function occur in fleeting intermediate states that are difficult to observe using conventional structural biology techniques. This limits our ability to fully understand how biological systems operate and respond to their environment.
 
My research focuses on developing new experimental approaches to capture these dynamic processes as they happen. Using time-resolved crystallography, my work combines ultrafast X-ray measurements with light-triggered reactions to take a series of structural snapshots of a protein as it changes over time. These snapshots can be assembled into ‘molecular movies’ that reveal how biological function emerges from structural motion.
 
A key innovation in my work is the development of Hadamard time-resolved crystallography (HATRX), a new approach that enables multiple time points to be encoded and measured simultaneously within a single experiment. This overcomes fundamental limitations of conventional methods, significantly improving efficiency and allowing access to systems that were previously too fast or too complex to study.
 
By integrating crystallography with complementary spectroscopic techniques and advanced data analysis, my research provides a more complete picture of biomolecular dynamics. This allows previously hidden intermediate states to be identified and offers new insight into the mechanisms that underpin biological function.
 
This work has broad implications for fields ranging from enzymatic catalysis to light-driven biological processes, helping to bridge the gap between experimental observation and molecular simulation. Ultimately, it aims to transform our understanding of dynamic molecular systems and enable the rational design of new molecules and materials with tailored function.

Who or what first sparked your interest in chemistry, and how has that interest evolved over time? 

My mum was the first person to spark my interest in science. Whenever I asked questions, she would give me the real answer rather than a simplified one, which challenged me to think more deeply and take my curiosity seriously. Although she left school at 16, she later studied part time for an Open University degree in mathematics and I am still amazed by her motivation. 

What began as a general interest in science has developed into a focus on understanding how fundamental principles can be applied to develop new experimental tools, particularly for studying dynamic molecular systems.

What has been the most rewarding or memorable highlight of your career so far? 

Experiments at XFEL facilities have been a particularly rewarding highlight of my career. Working as part of large international teams, and closely with dedicated beamline scientists who ensure that complex experiments run smoothly, has been both inspiring and highly collaborative. It is during these experiments that I have been most proud of my graduate students, Jake Hill, Diana Gaman, and Yelyzaveta Pulnova, who have demonstrated exceptional teamwork, even under demanding conditions.

What have been the biggest challenges that you have faced over the course of your time in science, and what have you learned from those experiences? 

A major challenge has been pushing experimental methods beyond their established limits, particularly in time-resolved measurements at large-scale facilities. These experiments are inherently uncertain and often require balancing ambition with practicality. This has taught me to embrace uncertainty as part of the scientific process, and to value persistence, teamwork, and careful problem-solving.

Thinking back to earlier in your career, are there any words of wisdom that you wish someone had told you? 

To embrace uncertainty. Some of the most important developments come from unexpected outcomes that shift the direction of your work.

What impact would you say that your work is having on your field and/or the wider world? 

My work focuses on developing new approaches to time-resolved crystallography, enabling the direct study of molecular dynamics. By reducing experimental barriers, it contributes to democratising access to these methods, allowing a wider range of researchers to engage with dynamic structural measurements. This supports a broader shift in structural science from static descriptions towards a real-time understanding of molecular function.

What future directions or opportunities do you see for your work? 

A key opportunity is to apply my approaches to imaging, enabling in situ observation of dynamics in complex systems. By linking imaging, crystallography and spectroscopic techniques, molecular processes can be understood across a broad range of time and length scales.

What do you wish more people understood about your field or the chemical sciences in general? 

That there is no single route into science, and that diverse perspectives are essential to progress. In particular, by placing a greater emphasis on accessibility in experimental design we can ensure that disability is not a barrier to participation.

In what ways does creativity influence how you think about or carry out your work? 

Creativity plays an important role in how I think about data, especially through my love of music. Through a data sonification project, I have explored how representing data as sound can reveal patterns in a different way, drawing on ideas from music such as rhythm and structure.

Are there any scientific developments, either recent or on the horizon, that you are excited about? 

I am particularly excited by developments in protein design, especially the ability to create proteins with bespoke, light-driven functions. Time-resolved crystallography provides a powerful way to understand how these systems behave in real time and to guide their design.

What does good research culture mean to you, and why does it matter? 

To me, a good research culture encourages participation from all levels and creates space for healthy debate and constructive discussion. Collaboration is key, we are all continually learning and a positive culture allows us to grow together.

How can scientists try to improve the environmental sustainability of research? Can you give us any examples from your own experience or context? 

Scientists can improve the environmental sustainability of research by reducing travel, optimising resource use, and making greater use of shared facilities. In crystallography, remote access to large-scale facilities allows experiments to be carried out without the need for travel, while automation can improve how efficiently beamtime and samples are used. For example, facilities such as Diamond Light Source have made significant progress in enabling remote experiments, demonstrating how these approaches can reduce environmental impact while maintaining high quality research.

How important would you say collaboration is for producing high quality science? How has collaboration influenced your work? 

Collaboration is essential for producing high quality science, particularly in large-scale experiments such as those at XFEL facilities. These projects rely on large international teams and often run on goodwill, with contributions from many individuals working together towards a common goal. In my work, collaboration with facility scientists and international collaborative teams has been central to both developing new methods and successfully carrying out these experiments.

If you had unlimited resources, what research question would you most want to explore? 

With unlimited resources, I would explore the application of ghost imaging to structural and time-resolved measurements. This approach, which reconstructs images from correlated signals, could provide new ways to study complex or radiation-sensitive systems.

What is your favourite element and why? 

Sulfur is definitely my favourite element, it is so versatile and important across chemistry and biology. Its ability to exist in multiple oxidation states and participate in photochemical processes makes it really exciting to study.