x-ray crystallography

Drug zeroes in on mutated nuclear receptors found in cancer, leaves normal proteins alone

With the aid of X-ray crystallography, researchers at the University of Michigan have revealed the structures of two closely related enzymes that play essential roles in the body's ability to metabolize excess lipids, including cholesterol.

Facing a challenge akin to solving a 1,000-piece jigsaw puzzle while blindfolded—and without touching the pieces—many structural biochemists thought it would be impossible to determine the atomic structure of a massive cellular machine called the nuclear pore complex (NPC), which is vital for cell survival.

Laboratories at The Scripps Research Institute (TSRI) are investigating antibodies to fight Ebola virus, including the three antibodies recently used to treat two American health care workers infected with the Ebola virus.

High resolution X-ray crystallography is an imaging technique in which X-ray beams are shot through purified, crystallized proteins. The beam scatters in different directions, allowing scientists to construct a detailed, 3-D model of the crystallized protein's molecular structure. Measuring the intensities and angles of the diffracted beams reveals the position of each atom in the protein.