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Research Digest Synopses of Research Articles Structure of Aquaporin Reveals Mechanism for Transport Selectivity Biochemists aren’t much accustomed to seeing their work in After fabricating and growing a recombinant form of AqpZ in the popular press, save for annual coverage of the Nobel prize E. coli, David Savage in the Stroud group recovered the proteins in chemistry. This year, Roderick MacKinnon was recognized for from the bacterial colonies, then purified and concentrated them. working out the atomic structure of an ion channel and Peter The proteins were crystallized—capturing five water molecules Agre for discovering that a major protein found in red blood cells inside—and then analyzed by state-of-the-art high-resolution functions primarily as a water channel. Agre went on to establish X-ray diffraction techniques. The architecture of aquaporin Z, the the family of related channels, which he named “aquaporins.’’ researchers report, is typical of aquaporins, with a spiral of eight Channel proteins have aqueous pores that cross the cell oxygens providing water-binding sites inside the channel and membrane and regulate the amino acid side chains determining the size and flow of molecules in and chemistry of the channel. The outer out of cells. Water passively membrane and cytoplasmic pours though aquaporins by ends of the channel are osmosis, moving from low