Diamond has been delivering intense beams of synchrotron light to scientists working at the forefront of research for the past nine years. During this time, the facility has steadily expanded from seven operational beamlines in 2007 to 27 at the start of 2016.
The success of large science facilities such as Diamond is measured in a variety of ways. Funders, stakeholders and those running the facility are continually monitoring the quality and quantity of the science that is published as a result of research conducted on the beamlines. The impact this science is having on the economy and society as a whole is also of great interest, as is the contribution the facility makes to the wider scientific landscape in terms of large collaborative projects, such as the new electron microscopy facilities and bringing scientists from different disciplines together to advance science in novel ways.
Towards the end of 2015, Diamond reached two important milestones with respect to scientific output. The 3,000th protein structure to be solved at the facility was deposited in the Worldwide Protein Data Bank, of which Diamond is the third highest contributor globally, and the 4,000th paper published from Diamond research appeared in the journal Spectrochimica Acta Part B.
Scientists from the University of Leicester deposited the 3,000th protein structure to be solved at Diamond in the Worldwide Protein Data Bank in September 2015. They solved an elusive protein called pneumolysin and their findings were published in Scientific Reports. Pneumolysin, a toxin secreted by Streptococcus pneumoniae bacteria, is capable of killing cells. In doing so, it helps these bacteria, which are responsible for a range of serious illnesses including pneumonia, meningitis and septicaemia, to take hold in humans.
L-R: Peter Moody, Russell Wallis, and Peter Andrew from the University of Leicester on the I04-1 beamline where Diamond's new fragment screening facility is based. Russell holds a 3D print of the crystal structure of pneumolysin.
Russell Wallis, one of the lead researchers, explains: “We wanted to uncover how pneumolysin kills our cells, thereby causing tissue damage and contributing to disease. In particular, we wanted to find out how multiple copies of the toxin assemble on the surface of cells.”
“Using Diamond’s crystallography beamlines, we’ve been able to determine the full-length pneumolysin at high-resolution. Down at this level, we can study the molecular interactions taking place on the cell membrane and work out exactly how the protein forms the pores that are lethal to the body’s cells. Having this knowledge is very exciting as it forms the basis for rational approaches to designing drugs that block assembly of pneumolysin pores to treat people with pneumococcal disease. Leicester has recently set up a company, Axendos Therapeutics, to pursue this aim.”
Marshall et al. The Crystal Structure of Pneumolysin at 2.0 Å Resolution Reveals the Molecular Packing of the Pre-pore Complex. Sci Reports (2015). DOI: 10.1038/srep13293
An international group of scientists from Poland, Austria, and the UK used Diamond’s X-ray fluorescence capabilities to advance our understanding of the changes taking place during the progression of brain cancer. This research, which is also the 4,000th paper to be published based on data collected at Diamond, may lead the way to a new tumour assessment method which could complement traditional approaches.
Distribution of calcium, sulfur and iron in a section of diffuse astrocytoma, courtesy of Wandzilak et al.
Changes in metal distribution in the brain have been linked to the degree of malignancy of brain cancer. With results published in Spectrochimica Acta Part B, the researchers found that trace metals could be used to correctly identify cancerous tissue in over 99% of cases and effectively classify the cancer stage.
Andrew Harrison, Diamond’s CEO, comments: “I’m delighted that Diamond’s 4,000th paper so aptly demonstrates the impact that synchrotron research can have on people’s lives. This work is still in its early stages but, in time, the discovery of the link between certain trace metals and their role in the growth of cancer cells could help to redefine the way we identify brain tumours, allowing for earlier diagnosis and, ultimately, a better chance for patients.”
Since Diamond first opened its doors to the scientific community, it has strived to keep the UK at the forefront of research by providing world class facilities and specialist support to the 8,000 scientists who choose Diamond for their synchrotron experiments. Panels of external experts allocate beamtime to those proposing science of the highest quality. Through a highly successful user focused service, Diamond helps researchers to realise their experimental aspirations, delivering data that leads to published papers in high impact journals. The rate at which protein structures are solved at Diamond makes the facility one of the top synchrotrons in the world for the number of structures deposited in the Protein Data Bank.
Andrew Harrison concludes: “Diamond will continue to develop and grow, achieving additional milestones along the way. We want an increasing number of scientists to be able to further their research using cutting-edge synchrotron capabilities so that they can deliver exciting, world leading science that continues to have a positive impact on society as a whole.”
Wandzilak et al. X-ray fluorescence study of the concentration of selected trace and minor elements in human brain tumours. Spectrochim Acta B. (2015). DOI:10.1016/j.sab.2015.10.002
Diamond Light Source is the UK's national synchrotron science facility, located at the Harwell Science and Innovation Campus in Oxfordshire.
Copyright © 2018 Diamond Light Source
Diamond Light Source Ltd
Harwell Science & Innovation Campus