Aided by the brilliant X-rays produced by synchrotron radiation at the Argonne National Laboratory in Illinois, a group of scientists from Northwestern University have determined the complete molecular structure of the copper chaperone for superoxide dismutase (CCS) ("Heterodimeric structure of superoxide dismutase in complex with its metallochaperone," Nature Structural Biology, 8:51-5, Sept. 2001). The metallochaperone's structure was known except for the third domain. Now, researchers suspect, through genetic evidence and structure, that this armlike structure is responsible for delivering copper to its target protein, zinc superoxide dismutase (SOD1). When CCS docks with SOD1, the arm becomes more ordered in its interaction. By using X-rays that are many magnitudes brighter than normal, this domain could be clearly viewed. Synchrotron radiation is 10 orders of magnitude, or 10 billion times more brilliant, than the standard laboratory X-ray source. According to Amy Rosenzweig, assistant professor of biochemistry, molecular biology, and cell...
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