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100 years of crystallography. You have full access to this article via your institution. Download PDF In 1914, German scientist Max von Laue won the Nobel Prize in Physics for discovering
how crystals can diffract X-rays: a phenomenon that led to the science of X-ray crystallography. Since then, researchers have used diffraction to work out the crystalline structures of
increasingly complex molecules, from simple minerals to high-tech materials such as graphene and biological structures, including viruses. With improvements in technology, the pace of
discovery has accelerated: tens of thousands of new structures are now imaged every year. The resolution of crystallographic images of proteins passed a critical threshold for discriminating
single atoms in the 1990s, and newer X-ray sources promise images of challenging proteins that are hard or impossible to grow into large crystals. BIRTH OF AN IDEA Credit: SPL Von Laue hit
on the idea that when X-rays passed through a crystal, they would scatter off the atoms in the sample and then interfere with each other like waves passing through a breach in a shore wall.
In some places, the waves would add to each other; in others, cancel each other out. The resulting diffraction pattern could be used to back-calculate the location of the atoms that
scattered the original X-rays. Von Laue and his colleagues proved his theory in 1912 with a sample of copper sulphate. GOING UP The Worldwide Protein Data Bank has been collecting resolved
structures of proteins since 1971, and now holds nearly 100,000 entries. Other databanks, including the Crystallography Open Database (COD), include structures of everything from minerals to
metals and small biological molecules. The COD is now adding instructions into its database for how to print three-dimensional models of some structures. Credit: Source: Worldwide Protein
Data Bank/ Crystallography Open Database GETTING CLEARER Better techniques for both imaging and interpreting data have allowed researchers see finer details in some structures and tackle
ever more complicated molecules. Credit: Images: Bernhard Rupp/Garland Science/Taylor & Francis Graph: H. M. Berman Protein Sci. 21, 1587–1596 (2012), with updates from Worldwide Protein
Data Bank 100 YEARS OF CRYSTALLOGRAPHY 1913: DIAMOND Diffraction image allowed researchers to confirm the tetrahedral structure of carbon atoms in this famous crystal. 1923:
HEXAMETHYLENETETRAMINE The first organic molecule to be imaged, chosen because of its simple cubic symmetry. It proved that molecules, not just atoms, can make up the repeating elements of a
crystal. Credit: Am. Chem. Soc. 1925: QUARTZ The determination of the structure of silicate minerals was fundamental to the field of mineraology. 1952: DNA Rosalind Franklin’s X-ray image
of DNA, known as photo 51, helped James Watson and Francis Crick to create their famous model of the double helix. An atomic-resolution image of the structure proposed in 1953 was not taken
until 1980. Credit: King’s College London 1958: MYOGLOBIN The irregular folds seen in the structure of the first imaged protein were a huge surprise. 1965: LYSOZYME The first enzyme to be
imaged, sourced from hen egg whites. 1970: SYNCHROTRON A study of insect muscle at the German Electron Synchrotron (DESY) in Hamburg was the first to use X-rays generated by a synchrotron.
The use of these machines caused a boom in crystallography studies. 1978: TOMATO BUSHY STUNT VIRUS First atomic-scale image of a complete virus: in this case, a plant virus. It revealed
structural rules that were found to hold true in human pathogens a few years later. 1984: QUASICRYSTALS The first crystals were identified with atomic arrangements that do not repeat
exactly, defying general wisdom about crystals. Credit: US Dept of Energy/AFP/Getty 2000: RIBOSOME The molecular machine that assembles proteins from instructions encoded in DNA. Credit: V.
Ramakrishnan & D. E. Brodersen/Medical Research Council 2009: X-RAY FREE-ELECTRON LASER The Linac Coherent Light Source at the SLAC National Accelerator Laboratory in Menlo Park,
California, went into operation, opening up a new world of imaging possibilities (see page 604). 2013: HIV TRIMER An X-ray crystallographic image of the hook that HIV uses to bind to human
cells helped to resolve a debate about what this important protein looks like. Credit: AAAS THE FUTURE The ‘most wanted’ list of proteins that remain to be imaged includes the massive
spliceosome, which helps to organize and edit messenger RNA, and the even larger nuclear-pore complex, which serves as a nucleus’s gatekeeper. These structures can contain hundreds of
proteins, making them hard to crystallize or keep still for an image. One strategy is to crystallize bits of these structures and piece them together like a jigsaw; the use of X-ray
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AQ~~,AAAAAFNl7zk~,OmXvgxJOvrFZYqSlJuZl7DkhsNbEfjvA * @videoPlayer: 3117749322001 * isVid: true * isUI: true * dynamicStreaming: true Authors * Nicola Jones View author publications You can
also search for this author inPubMed Google Scholar RELATED LINKS RELATED LINKS IN NATURE RESEARCH Molecular structures: The crystal century 2014-Jan-29 X-ray science: The big guns
2014-Jan-29 Femtosecond X-ray protein nanocrystallography 2011-Feb-02 X-ray free-electron lasers fire up 2009-Oct-07 Protein structures: Structures of desire 2009-May-06 _Nature_ special:
Crystallography at 100 RELATED EXTERNAL LINKS International Year of Crystallography RIGHTS AND PERMISSIONS Reprints and permissions ABOUT THIS ARTICLE CITE THIS ARTICLE Jones, N.
Crystallography: Atomic secrets. _Nature_ 505, 602–603 (2014). https://doi.org/10.1038/505602a Download citation * Published: 29 January 2014 * Issue Date: 30 January 2014 * DOI:
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