Protein Crystallography with Neutrons Featured in Physics Today


Research at the new protein crystallography station at the Los Alamos Neutron Science Center (LANSCE) has demonstrated that neutron crystallography can reveal information about the structure of proteins that is not accessible by x-ray crystallography. A scientific team led by Gerald Bunick of the Oak Ridge National Laboratory (ORNL), and including researchers from the University of Tennessee, the Fox Chase Cancer Center, and the Los Alamos National Laboratory has determined the precise arrangement of hydrogen atoms on key amino acids of the enzyme D-xylose isomerase. This protein is a bimetallic enzyme that catalyzes the conversion of glucose into fructose by hydrogen atom transfer. It is widely used in the manufacture of high-fructose corn syrup for use in foods. Understanding the structure of the enzyme could lead to design of a modified enzyme that is more efficient in the production of fructose from glucose. Information obtained through neutron crystallography will enhance our knowledge of the mechanism of proton transfer in enzymes of this type as well as in other related enzymes involved in several important metabolic pathways. The new study is highlighted in an article about neutron crystallography of proteins in the November 2003 issue of Physics Today. A scientific paper on the research has just been accepted for publication in Acta Crystallographica D.