NDSU researchers are marking the centenary of the development of one of the major techniques in modern science: x-ray crystallography. The United Nations Educational, Scientific and Cultural Organization has declared 2014 as the International Year of Crystallography.
The discipline has provided contributions to such diverse disciplines as physics, medicine and materials sciences, and the International Union of Crystallography is participating in an effort to raise awareness and support for the field.
Leading research is being conducted at the NDSU Department of Chemistry and Biochemistry's Materials Characterization Laboratory, which is managed by staff scientist Angel Ugrinov. The lab provides area researchers access to multiple X-ray diffractometers for data collection for structure solution from single crystals or powders. In 2013, the laboratories of Christopher Colbert, assistant professor of chemistry and biochemistry, and Sangita Sinha, assistant professor of chemistry and biochemistry determined and deposited into the International Protein Data Bank the first high-resolution protein structures solved in North Dakota. The structures provide insights into the role of various proteins involved in signaling during brain injury and the regulation of autophagy, a cellular nutrient recycling pathway. Publications are forthcoming on their research.
Contributions by crystallographers often fall under the realm of basic research. However, crystallography is increasingly a driving force behind applied research in such areas as structure-based drug design, determination of enzymatic mechanisms and elucidation of protein-protein interactions.
The history of the field dates back more than a century.
In 1914, German physicist Max von Laue won the Nobel Prize in Physics for his discovery that crystals diffract X-rays in mathematically predictable ways. The father-son team of William Henry Bragg and William Lawrence Bragg shared the 1915 Nobel Prize in Physics for expanding upon von Laue’s work. The Braggs provided the mathematical framework for accurately deducing the atomic structure of a crystal through analysis of the diffraction pattern produced by reflected X-rays.
Since the early work of the Braggs on simple crystalline compounds like table salt and diamond, X-ray crystallographers have tackled increasingly complex systems in an effort to understand how the underlying atomic structure of a compound – a mineral, drug, protein, DNA or viruses – determine how that compound functions or interacts with others.
Since the 1901 Nobel Prize in Physics was awarded to Wilhelm Conrad Rontgen for the discovery of X-rays, 48 Nobel Prizes in physics, chemistry, physiology or medicine have been awarded for scientific achievements associated with or directly involving the utilization of crystallographic techniques.
For more information concerning the International Year of Crystallography and various resources pertaining to crystallography, visit http://www.iycr2014.org/about and http://www.richannel.org/celebrating-crystallography.
NDSU is recognized as one of the nation's top 108 public and private universities by the Carnegie Commission on Higher Education.