Skordalakes' lab deciphered a key part of beetle telomerase, an enzyme that can enhance or hinder a cell's ability to multiply limitlessly. The catalyst plays an active role in at least 85 percent of all cancers.
"Knowing the atomic structure of one of these little molecular machines is a breakthrough that enables and facilitates future research," said Thomas R. Cech, who shared the 1989 Nobel Prize in chemistry for discovering catalytic properties of RNA. As basic science, he said, "this is a technical tour de force."
The science is so basic that the hurdles ahead are too numerous to name. But so are the potential payoffs.
Like a shoelace, a strand of DNA frays at the ends if exposed. Shoelaces are shielded by plastic caps. DNA is protected by sections at each end called telomeres.
But every time the DNA double helix makes a copy of itself in cell division, the telomeres get shorter.
In this role, telomeres actually operate more like the bottom of a shoe - able to lose a lifetime's worth of layers before the essentials inside become imperiled.
That's fine for most cells most of the time. But in cases that call for rapid cell replication - a developing embryo, for example, or a cancerous tumor - the telomerase machine kicks into gear, manufacturing new tracts of telomere to replace those that are fast disappearing.
Telomerase was discovered in the mid-1980s. Scientists around the world have been testing all sorts of molecules in hopes of finding some that could inactivate the enzyme and point toward new drugs. Not knowing the complex protein's exact structure - the dimensions of the hole for which they needed to locate a peg - made finding a fit daunting.
Researchers who tried to figure out that exact structure were just as frustrated, if not more so.
