2000年12月31日
筋小胞体カルシウムポンプの結晶構造解析
日本結晶学会誌
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- 巻
- 42
- 号
- 6
- 開始ページ
- 478
- 終了ページ
- 485
- 記述言語
- 日本語
- 掲載種別
- DOI
- 10.5940/jcrsj.42.478
- 出版者・発行元
- The Crystallographic Society of Japan
Calcium ATPase (Calcium pump) from sarcoplasmic reticulum is an integral membrane protein of Mr 110 K and a representative member of P-type ATPase involved in the active transports of ions with the energy from ATP hydrolysis. This ion pump regulates muscle relaxation by up-taking calcium ions from muscle cells into sarcoplasmic reticulum against the concentration gradient of the calcium. This ion pump has been successfully crystallized into ultra-thin plate crystals (<20 micron) by a dialysis method. Through the multiple-isomorphous replacement experiments at cryogenic temperature, the three-dimensional structure of this pump has been determined at a resolution of 2.6Å. The crystal structure is the first to reveal the structural architecture of P-type ATPase. Here, we describe the methods used for solving the phase problem in the crystal structure analysis for such ultra-thin plate crystal: combination of cryogenic X-ray diffraction experiments and cryogenic electron microscopy.
- リンク情報
- ID情報
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- DOI : 10.5940/jcrsj.42.478
- ISSN : 0369-4585
- CiNii Articles ID : 10007410631
- CiNii Books ID : AN00188364