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
About the International Year of Crystallography
A presentation by Michele Zema, IYCr2014 Project Manager at the International Union of Crystallography, describing the objectives of the Year and some of the major projects that are planned or in preparation.
Category: Science & Technology. Duration: 5m 27s
Licence: Standard YouTube Licence
The Royal Institution Crystallography Collection
Mars Diffracts! X-ray crystallography and space exploration
An epic journey into the role of X-ray diffraction in space
Astrobiologist and intrepid science communicator Lewis Dartnell reveals the crucial role that X-ray crystallography is playing in understanding the formation and history of our planetary neighbour, Mars.
Explaining the techniques used by the Curiosity Rover to analyse the Martian surface, Lewis reveals what the discovery of clay might mean for the possibility of life on the Red Planet.
Joined by space scientists responsible for designing and operating instruments over 60 million kilometres away, Lewis delves into the mysteries of interplanetary exploration including: How do you design reliable instruments for use on other planets? Should we send humans to Mars? And, what does the next mission to the Red Planet look like?
Featuring instrument scientist Graeme Hansford (University of Leicester) and John Bridges, a participating scientist with the NASA Mars Science Laboratory working on the current Curiosity mission.
This film was produced by Thom Hoffman and supported by the Science and Technologies Facilities Council (STFC).
Filmed: 2014. Duration: 11m 43s
Credits: Thom Hoffman
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
Sir Lawrence Bragg on crystals and gems
A series of six outside broadcasts filmed at the Royal Institution in the late 1950s and early 1960s, The Nature of Things was presented by William Lawrence Bragg with the assistance of Bill Coates. This is an extract from Crystals and Gems, the last show in the first series, exploring the properties and molecular structure of crystals.
Coates recalled Bragg once remarking to him: "never talk about science, show it to them", which is what The Nature of Things set out to do. Like the Christmas Lectures, the programmes were structured around a series of demonstrations and were filmed as a lecture in the Ri's theatre. Although the filming took place with an audience of adults, the series was aimed at children and broadcast on children's television. As he states at the end of the series, he hoped it would provoke "deep interest in the science of everyday things".
Broadcast on BBC Television in 1959. Duration: 17m 22s
© The Royal Institution. Credits: The Royal Institution /BBC