Here are a bunch of articles giving the overview of some fancy biochemistry research that allowed a chemokine and its receptor to be seen together for the first time. The interesting thing about this to me is that people in my lab were heavily involved in this.
Basically chemokines are proteins whose function and structure are well-enough understood. They sit on the outside of cells and bind to various chemical signals and, in response, activate changes inside the cell based on this input. They are like the external sensory aparatus at the level of cells. They are important for growth regulation (or lack thereof as in cancer), viral infections, and a bunch of other mission critical things.
What was not well understood was how these structures actually did what they were known to do. What was accomplished here was figuring out how to get this protein to be crystallized with its ligand (the ligand is the small signalling chemical that triggers the response). Once proteins are crystalized, their structure can (pretty much) be figured out using a technique that won the Nobel Prize in physics one hundred years ago. Previously, it was hard to get both the protein and the ligand into the same crystal structure. Our lab used computer models to try various tricks to stabilize the complex so that it would crystalize more easily. Once a good setup was found using computer tricks, the main wet lab working on the project tried the design in real biological material and it worked! The complex was crystallized together and the structure (i.e. the location in 3d space of all the atoms involved) was determined.
This lead to a much greater insight about how chemokine receptors really work. For example, it was not previously known if one signalling molecule was enough to trigger the recpetor. Now it is known that multiple signalling molecules are not required and that one signalling chemical is the typical way these proteins are activated.
"So what?" you might be thinking. It does sound pretty minor, certainly very tiny. But that’s where we’re at these days. Very tiny things are what we don’t know that can successfully be explored. In the mid 16th century, anatomists like Andreas Vesalius were revolutionizing human health by actually cutting open cadavers and taking a look in a systematic and documented way. At that time it was known that humans, like butchered animals, have bones but until an actual direct study of the connective tissue of humans was performed, how human skeletons actually worked was either not known or inferred incorrectly from other animals. Certainly at the time there was controversy suggesting that this line of research was not merely pointless, but perhaps unethical. Yet 450 years later, this work remains an important foundation to our extremely advanced understanding of macro structures in the human body.
The exploration we are doing now is at the level of individual atoms. As fantastic and remote as that may seem to our normal human perspective, it is in fact where the frontier of health science is today. The human body has around 50 trillion somatic cells which are mostly all covered with chemokine receptors. Although this process' mechanisms are invisible at our normal scale they are involved in a large variety of very serious real health consquences.
It may be that this work will not help someone today. It may not be of much use pragmatically in our lifetimes. But in 500 years, it is quite likely that these computer-assisted explorations of anatomical structures at the atomic scale will be the foundation of breakthroughs in medical technology that will revolutionize, for the better, how our species lives.