Protein Crystallography research is conducted at Synchrotron
Radiation facilities such as the National Synchrotron Light Source at
Brookhaven National Laboratory. Synchrotron Radiation is an intense
variety of electromagnetic radiation created by accelerating electrons.
In order to have the capability of resolving individual atoms, X-rays
must be used because of their short wavelength. X-ray beams are created
by the Synchrotron and then focused onto a protein crystal mounted in a diffractometer.
from the source, the Synchrotron beam line, pass through
the crystal and are then collected by the CCD detector. CDD
(charged couple device) detectors convert photons to digital images;
they are identical to the units found in digital cameras. In order
collect sufficient data to determine the structure of the protein, the
crystal must be rotated. The crystal mount is
automated and can rotate to within a fraction of a degree. A closed
circuit video camera monitors the status of the crystal and helps
align the crystal in the X-ray beam. Synchrotron X-rays are extremely
intense. When they strike protein molecules, they disrupt the molecular
bonds and cook the crystal. To prolong the life of the crystal, a jet of
liquid nitrogen from the cooling system keeps it at comfortable
100 degrees Kelvin.