Abstract
Through the use of electron crystallography, it has been possible to obtain high resolution structural information regarding a mammalian protein that spans the lipid bilayer. Two-dimensional crystals of the detoxification enzyme microsomal glutathione transferase were induced by slow detergent removal from a mixture containing low amounts of phospholipid. Images of specimens stabilized in tannin were collected using electron cryomicroscopy. The projection structure at 4 Å shows tightly packed trimers of the protein. Each of them contains an inner core of six parallel α-helices delineating a central low density region. The helical bundle is partly surrounded by elongated domains.
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Hebert, H., Schmidt-Krey, I., & Morgenstern, R. (1995). The projection structure of microsomal glutathione transferase. EMBO Journal, 14(16), 3864–3869. https://doi.org/10.1002/j.1460-2075.1995.tb00058.x
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