KMID : 0578319940040030273
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Molecules and Cells 1994 Volume.4 No. 3 p.273 ~ p.275
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Crystallization of ¢¥20S¢¥ Proteasome fro Rat Liver
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Hwang, Kwang Yeon
Kim, Kyeong Kyu/Chung, Chin Ha/Tanaka, keiji/Suh, Se Won
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Abstract
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The proteasome, or multicatalytic proteinase complex, is a major non-lysosomal proteinase of eukaryotic cells. Proteasomes are large (approximately 700 kDa), cylindrical particles, composed of four stacked rings of disks. Determination of the three-dimensional structure of proteasome by X-ray crystallography is necessary in order to understand the structure-function relationship at the molecular level. As a first step toward the structure determination, crystallization of `20S¢¥ proteasome from rat liver has been performed by the hanging drop vapour diffusion method at room temperature. Two crystal forms have been obtained using PEG 8000 as precipitant. The crystals grew at room temperature within 14 days to dimensions of 0.05 mm X 0.1 mm X 0.1 mm. To our knowledge, this is the first report of three-dimensional crystals on a eukaryotic proteasome.
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