Protein crystallography in International Year of Crystallography

Mariusz Jaskólski


The United Nations proclaimed 2014 as International Year of Crystallography. Unlike physics, chemistry or biology, crystallography is a rather narrowly defined science. It is, however, very powerful through its structure-penetrating methodology and interdisciplinary intergrowth with all other natural and life sciences. Evolved from a mineralogy-related subject, crystallography gained momentum with the discovery of Max Laue (1912) that X-rays can be diffracted by crystals. In the hands of the father-and-son team of the Braggs in England, this discovery became a powerful tool for unraveling the atomic structure of matter. Starting with simple chemical molecules and crystals, the method of X-ray crystallography has also been used for biological macromolecules and their complexes, such as viruses, biological machines and organelles. In a spectacular synergism, crystallography and technology have fueled their own advances. The most dramatic change happened, and is still happening, in the generation of powerful X-ray beams. Home sources are almost forgotten and even the most powerful synchrotrons are being dwarfed by the looming X-ray Free Electron Lasers. With brightness that makes our Sun look terribly pale, these sources will ultimately allow us to get rid of the final constraint: of the crystal. We are thus looking into crystallography without crystals, at nanometer scale and in femtosecond time. However, the principle of diffraction holds, and the goal is the same: to understand the processes of life through the elucidation of the atomic structure of matter, even if it is transient, dynamic, or otherwise delicate.


protein crystallography; International Year of Crystallography; structural biology; Data Protein Bank; synchrotron radiation; XFEL

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