| タイトル | Salt-induced aggregation of lysozyme: Implications for crystal growth |
| 本文（外部サイト） | http://hdl.handle.net/2060/19950012600 |
| 著者（英） | Wilson, Lori J. |
| 著者所属（英） | State Univ. of East Tennessee |
| 発行日 | 1994-10-01 |
| 言語 | eng |
| 内容記述 | Crystallization of proteins is a prerequisite for structural analysis by x-ray crystallography. While improvements in protein crystals have been obtained in microgravity onboard the U.S. Space Shuttle, attempts to improve the crystal growth process both on the ground and in space have been limited by our lack of understanding of the mechanisms involved. Almost all proteins are crystallized with the aid of a precipitating agent. Many of the common precipitating agents are inorganic salts. An understanding of the role of salts on the aggregation of protein monomers is the key to the elucidation of the mechanisms involved in protein crystallization. In order for crystallization to occur individual molecules must self-associate into aggregates. Detection and characterization of aggregates in supersaturated protein solutions is the first step in understanding salt-induced crystallization. |
| NASA分類 | SOLID-STATE PHYSICS |
| レポートNO | 95N19015 |
| 権利 | No Copyright |
| URI | https://repository.exst.jaxa.jp/dspace/handle/a-is/108794 |
