Crystallographic studies of ribosomes led to fundamental insight into the cell's protein synthesis, which is coupled to the proper reading of the genetic code. Ribosomes thus represent an essential, biological basic principle for all life as we know it. Ribosomes were long considered as an "unattainable" target for crystallographic studies, but this changed radically as new technology of Synkrotrons, detectors and computer programs were developed to handle crystals of such large and complex molecular sizes as ribosomes. Thus, we know in detail today that protein synthesis is catalyzed by RNA ("RNA makes protein") and, for example, how a large number of antibiotics inhibit this process specifically in bacteria, but not our own ribosomes.
The biochemist in a cell is also controlled by proteins. Membrane proteins are thus responsible for all transport of nutrients, ions and signals in and out of the cell, and are therefore also of paramount importance to life. Like ribosomes, they were long regarded as almost impossible to study with crystallographic methods, as they are difficult to handle outside the membrane's protective grease mantle, for which they are closely aligned. However, in recent years we have seen numerous major breakthroughs with new methods to crystallize membrane proteins and determine their three-dimensional structure, which has opened up a tremendous insight into the cell's specific and carefully regulated mechanisms to Transport substances and send signals back and forth over cell membranes and how these, for example. have been affected by disease mutations and by medicinal products.
Through the ages, Danish researchers have been very significantly involved in this use and development of crystallographic methods to investigate some of the most complex issues in biology, and today we also see that new biotech companies are firing from Crystallographic basic research.