Learn about crystallography through watching
Below are listed some interesting video clips, webcasts, television programmes and films that explain crystallography. Click on the large images to download a video file, watch the clip, or be directed to an external website. Click on the smaller images for more information.
A selection of videos from the International Year of Crystallography playlist on YouTube
UN Secretary General launches IYCr2014
United Nations, 20 January 2014 - Video message by UN Secretary-General Ban Ki-moon on the launch of the International Year of Crystallography 2014.
"This year marks the centenary of the birth of modern crystallography. We celebrate 100 years of ground-breaking advances.Crystallography is fundamental to understanding the structure of matter. It is critical for materials science, health care, agriculture and biotechnology. Today, crystallography is at the core of structural sciences, revealing the constitution of minerals and the molecules of life, helping scientists to design new-generation materials and life-saving medicine. In recognition of these important contributions, the United Nations General Assembly designated 2014 as the International Year of Crystallography.The goal is to raise awareness about the power of crystals, deepen cooperation and create new partnerships across the globe. Crystallography has an important place as we work for inclusive sustainable development - policies that are good for people and the planet. I thank UNESCO, along with the International Union of Crystallography and all other partners. Thank you for working to help societies harness the full power of sciences for sustainable development. Let us make the Year a great success!"
Category: News & Politics. Duration: 2m 13s
Licence: Standard YouTube Licence
The Royal Institution Crystallography Collection
An animated celebrationX-ray crystallography is arguably one of the greatest innovations of the twentieth century, but not that many people know what it is or how it came about. Join us on an animated journey through the 100 year history of crystallography – from the pioneering work of William and Lawrence Bragg in 1913 to the surface of Mars!
Narrated by structural biologist Stephen Curry and produced by animation company 12foot6, the film explores the extraordinary history of crystallography. To date 28 Nobel Prizes have been awarded to projects related to the field and X-ray crystallography remains the foremost technique in determining the structures of a huge range of complex molecules.
This film was produced in celebration of the Bragg Centenary and was funded by STFC.
Filmed: 2013. Duration: 3m 5s
Credits: 12foot6 / Royal Institution
License: © Royal Institution
Celebrating the International Year of Crystallography with methylation of Nod Factor
Each year, ~150 million tonnes of atmospheric nitrogen are converted to plant nutrients (eliminating the load of artificial fertilizers) by soil bacteria, called rhizobia, that live in symbiosis with legume plants, such as lupine. The association is highly specific and before it starts, the symbionts must recognize each other via exchange of precise chemical signals. The plant's root produces characteristic flavonoids, while the bacterial 'business card', called nodulation factor (NF), is an oligosaccharide molecule with a unique pattern of strange chemical decorations. The nodulation factor is named very adequately: once recognized, it will induce formation of root nodules, to be colonized by the bacterial partner. Rhizobia have unique biosynthetic pathways to produce NF, involving about a dozen of specialized proteins. One of them is NodS, an enzyme that decorates the Nod factor with a methyl group (CH3), transferred from a donor molecule called SAM. Dr. Ozgur Cakici, working at the Center for Biocrystallographic Research in Poznan (Poland), discovered the crystal structure of NodS and was able to elucidate its enzymatic mechanism, so elegantly shown in the movie. The enzyme starts with an open conformation, which allows docking of the SAM molecule. Upon SAM binding, the protein conformation changes dramatically, burying the donor molecule and forming a docking platform for the NF acceptor. When the NF molecule completes the tripartite complex, the methyl group gets transferred, and the products can depart the enzyme. The last component to leave is SAH, a molecule generated from SAM by methyl group removal. The open NodS molecule is ready to start a new catalytic cycle.
To solve the structure of NodS and of its complex with SAH, Ozgur first genetically modified bacterial cells for production of the protein in a variant containing selenium (Se) atoms. Crystals of that protein were taken for diffraction experiments to a synchrotron center that provided an extremely powerful X-ray beam with tunable wavelength. The experimental data were the basis for structure determination, which utilized the method of multiwavelength anomalous diffraction (MAD).
Dr. Cakici's results were published in Acta Crystallographica (Acta Cryst. F64, 1149-1152, 2008) and in the Journal of Molecular Biology (J. Mol. Biol. 404, 874-889, 2010).
Duration: 1m 58s
© Center for Biocrystallographic Research, Poznan
Crystallographers in Conference 1965
During the 1965 International Conference on Crystallography held in Melbourne, the opportunity was taken to record some of the great figures in the history of this subject. The twin topics forming the discussion basis for the conference were electron diffraction and the nature of defects in crystals. Among the distinguished scientists present, many had made special contributions to the research on those topics - had, in fact, pioneered a place for themselves in the story of crystallography.
Filmed at the International Crystallography Conference, 1965, Melbourne, Australia, by the CSIRO Film Unit in collaboration with the Australian Academy of Science. With support from UNESCO, the International Council of Scientific Unions, the Australian Academy of Science, the International Union of Crystallography, the International Union of Pure and Applied Physics, the International Atomic Energy Agency and the University of Melbourne.
Category: Science & Technology. Duration (complete programme): 41m 44s
Licence: Standard YouTube Licence