Author: Ward Smith

A crystal of hen egg white lysozyme. Credit: Alex McPherson, University of California, Irvine.

As you may know from the coverage in various popular news outlets and science journals (see below for a list), the United Nations Educational, Scientific and Cultural Organization has declared 2014 to be the “International Year of Crystallography .” This is in recognition of the 100th anniversary of the Nobel Prize in physics to Max von Laue for the discovery of diffraction of X-rays by crystals.

I first learned about crystallography in college, when I took a course in physical chemistry that included an introduction to chemical crystallography. Crystallography combines math, computer science, chemistry and biology—and that’s what convinced me to do graduate work in the field. When you determine structures, you’re often the first person to ever see that molecule, and that’s pretty exciting.

Since 1914, scientists have made many advances in the use of X-rays for the atomic-level determination of the 3-D structure of molecules. For instance, in the early years of the 20th century, William and Lawrence Bragg, father and son, learned that the newly discovered X-ray radiation could be used to locate the atoms in a crystal of matter. Their work ultimately led to Bragg’s Law for understanding X-ray diffraction and the structure determination of materials ranging from table salt to the ribosome. Breakthroughs made possible by crystallography (and diffraction) have led to 15 Nobel Prizes, including 7 with NIGMS support.

X-ray crystallography has impacted all areas of science, including biomedical research. The first biological finding was made by James Sumner, who discovered that enzymes could be crystallized (urease was the enzyme). In the years following, X-ray diffraction and crystallography have been used to reveal the structure of DNA and countless proteins and enabled structure-based drug design efforts. Crystallography has become an established tool of small molecule and protein studies.

Today, modern biological crystallography is practiced at synchrotron facilities, with access to 20 X-ray crystallography beamlines supported entirely or in part by NIGMS. Efforts are under way to make smaller, more intense beamlines that will allow the study of small crystals. Crystallography is also very much a part of the new X-ray laser facilities, where several NIGMS investigators are carrying out pioneering research on very small crystals of proteins, including membrane proteins, on X-ray scattering of proteins in solution and on protein dynamics.

Clearly, crystallography continues to be a cutting-edge field, and I’m excited to see what advances it brings during the coming years.

Articles about the International Year of Crystallography:

January 30 Special Issue of Nature 
UN to Raise Awareness of Little-Known Science Behind DNA, Computer Memory, New Drugs
2014 Is the International Year of Crystallography (‘What’s Crystallography?’ You Ask) 

A special symposium marking the 40th anniversary of the Protein Data Bank (PDB) will be held this year at Cold Spring Harbor Laboratory in New York, October 28-30.

It’s quite fitting that the meeting is being held here. It was a 1971 symposium at the laboratory titled “The Structure and Function of Proteins at the Three-Dimensional Level” that led to the establishment of the PDB as a freely accessible portal for the experimentally determined structures of biological macromolecules. Since then, the PDB has grown into an international resource for structural biology, today containing nearly 75,000 structures of proteins, nucleic acids and complex assemblies.

Because it is such a vital resource for researchers, NIGMS and other parts of NIH, along with the National Science Foundation and Department of Energy, have helped fund the PDB’s operation for many years. NIGMS is also a sponsor of the symposium.

The October event, which is open to all, will include presentations by many prominent scientists who have been instrumental in the development of the PDB and the field of structural biology. Among the confirmed speakers are Michael Rossmann of Purdue University, an early advocate of the PDB; Wayne Hendrickson of Columbia University, a leader in solving the structures of membrane proteins; and Kurt Wüthrich of the Scripps Research Institute and the ETH Zürich, a pioneer in NMR structure determination techniques.

A limited number of travel awards to attend the symposium are available for students and early career scientists; applications are due by
August 1.

More information about the program, registration and travel is on the meeting Web site.