To celebrate the International Year of Crystallography 2014, the Institute of Advanced Studies and the School of Chemistry and Biochemistry are pleased to present this special lecture series, which aims to promote the general understanding of Crystallography in the wider community.
The International Year of Crystallography 2014 commemorates not only the centennial of X-ray diffraction, which allowed the detailed study of crystalline material, but also the 400th anniversary of Kepler’s observation in 1611 of the symmetrical form of ice crystals, which began the wider study of the role of symmetry in matter.
This series, based at UWA, will feature three key lectures from our experts in the field:
Alice Vrielink, Professor of Structural Biology, School of Chemistry and Biochemistry, The University of Western Australia.
The science of crystallography has had an enormous impact on our understanding of molecules, their structures, chemical and physical properties. The impacts of crystallography are felt daily on how we live our lives. Nowhere is there more evidence of this than in the area of biology. Not long after the first Nobel Prizes were awarded to Max von Laue in 1914, and the father and son team of William Henry and William Lawrence Bragg in 1915 was crystallography applied to the studies of a diverse range of biological molecules. Early work by Hodgkin on the structures of cholesterol, penicillin and vitamin B12 provided important insights into how these molecules functioned. The birth of the field of molecular biology was a direct consequence of the discovery of the double helical structure of DNA by Watson, Crick, Wilkins and Franklin. The first protein structures determined by Perutz and Kendrew opened the field of macromolecular crystallography. Subsequent structural studies of biomolecules have helped us understand fundamental biological processes such as how muscles contract, how cells divide, how proteins are made within the cell and how signals are transmitted and received between cells and tissues within our bodies. Crystallography has also helped us understand disease processes and design new and effective therapeutic agents to treat diseases and illnesses. In this lecture Professor Vrielink will give an overview of the impact crystallography has had in the area of biology and medicine. She will describe the seminal discoveries as a result of crystallographic studies of biological molecules and how these discoveries are helping us to understand the mysteries of life.
Mark Spackman, Winthrop Professor and Head, School of Chemistry and Biochemistry, The University of Western Australia.
We all know what crystals are, but how much do we know about what lies within? And how do we know it? This year celebrates the centenary of X-ray crystallography, but attempts to understand the relationship between the external form of crystals, and the arrangement of the particles within, date back to some remarkable insights made by Kepler, Hooke and Huygens in the 17th century. Real progress in understanding the structure, shape and properties of the ‘globules’ or ‘corpuscles’ from which crystals were thought to be built had to wait until the 19th century, with the foundations of modern stereochemistry. The development of atomic theory and quantum mechanics in the early 20th century, coupled with the discovery of X-ray diffraction, enabled the first experimental verification of the regular periodic arrangements of particles in crystals. The vast number of crystallographic studies that followed have provided extraordinary detail on the three-dimensional arrangement of atoms in molecules and crystals, and especially the way molecules interact and arrange themselves to form crystals. In this lecture Professor Spackman will trace some of this fascinating story, partly from the viewpoint of his novel partitioning of crystals into discrete molecular fragments, and the development of software now used worldwide for the identification, analysis and discussion of intermolecular interactions in molecular crystals. The link between this modern perspective and very early ideas on the internal structure of crystals will be presented through several studies on molecular crystals that have become landmarks in the development of modern X-ray crystallography.
Stephen Curry, Professor of Structural Biology, Imperial College London.
Just over a hundred years ago a narrow beam of X-rays was fired at a crystal for the very first time. The experiment, an early attempt to investigate the nature of this recently-discovered radiation, showed that it was wavelike and so constituted a new type of of light. Although that was in itself a profound discovery, scientists realised immediately that the far more interesting outcome of the experiment was the revelation that X-rays could be used to ‘see’ the atomic structure of matter in three dimensions at a level of detail beyond the reach of even the most powerful microscopes. The technique of X-ray crystallography, first used to work out the atomic structure of simple crystals and minerals, has since been applied to the far more elaborate molecular structures found in chemistry and biology. It is arguably one of the greatest scientific advances of the 20th century. In this lecture Professor Curry will recount the curious origin of the technique (including its Australian roots), explain how it works and discuss how crystallography opened up an entirely new landscape for scientists to explore.