Protein structures make an appearance at Cheltenham Science Festival

The rise of antibiotic resistant bacteria and the centenary of the birth of X-ray crystallography were topics explored at this year’s Cheltenham Science Festival with assistance from the department’s Professor Elspeth Garman.

Image courtesy of Diamond Light Source

Image courtesy of Diamond Light Source (Click to enlarge)

Run by Pfizer and Diamond Light Source respectively, the two events attracted large and enthusiastic audiences and stimulated a wide range of questions.

Whilst there, Elspeth was invited to join science journalist and presenter Quentin Cooper. Their discussion about the history and future of X-ray crystallography was broadcast on Radio 4’s ‘Material World’ (www.bbc.co.uk/programmes/b02147xp).

Public health expert Anthony Kessel, medical microbiologist Mark Wilcox, and Chair Suzy Lishman from the Royal College of Pathologists shared the stage with Elspeth for the discussion about antibiotic resistance. Elspeth used beads and models as props to explain at a molecular level how antibiotics work against their bacterial targets and how resistance can develop. 

Despite a reduction in the number of cases of MRSA and other life-threatening infections in the UK, we are poorly equipped to deal with new infections. The panel discussed about the challenges of developing new antibiotics and the impact of GPs’ prescribing habits - including the suggestion, raised by one member of the audience, that GPs prescribe placebos instead.  

‘Bragging about Crystallography’ took place on the same day at the Festival. Elspeth and structural biologist Tom Blundell took the audience through the history of X-ray crystallography in the 100 years since the Bragg equation, which made the technique possible, was described.

Father and son team William Henry and William Lawrence Bragg were responsible for the Bragg equation and the development of the methodology for linking diffraction pattern to sample structure. This meant that scientists could freeze their sample and determine its structure from the diffraction pattern of the crystals.

Image courtesy of Diamond Light Source

Image courtesy of Diamond Light Source (Click to enlarge)

Following the creation of Bragg’s Law, the two men used their new technique to solve the structure of a number of crystals including sodium chloride. They received the Nobel Prize for Physics in 1915 when Lawrence Bragg was only 25.

Elspeth talked about how the Braggs’ pioneering work has formed the basis of structural research in modern science. Showing crystals of all shapes and sizes, including 12 metre long crystals found in Mexico, she explained how scientists use Bragg’s Law to 'read' a pattern of diffraction spots on the X-ray detector. With further calculations, they can deduce the folding of amino acids in the protein.

X-ray crystallography has been used to understand the structure of a vast number of proteins – around 90,000 to date. Elspeth explained how the technique has provided crucial information for drug development. The design of the anti-flu drug Relenza, for example, was based on the crystal structure of flu neuraminidase protein which it targets.

Sitting in the audience were Jim Watson and Lawrence Bragg’s daughter, Patricia Thompson. She publically thanked Jim Watson for asking her father to write the foreword of ‘The Double Helix’ which she said had been an honour for him. 





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