Crystal Structure Analysis of Calcium Pump from Sarcoplasmic Reticulum.

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  • NAKASAKO Masayoshi
    Institute of Molecular and Cellular Biosciences, The University of Tokyo
  • NOMURA Hiromi
    Institute of Molecular and Cellular Biosciences, The University of Tokyo
  • OGAWA Haruo
    Institute of Molecular and Cellular Biosciences, The University of Tokyo
  • TOYOSHIMA Chikashi
    Institute of Molecular and Cellular Biosciences, The University of Tokyo

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  • 筋小胞体カルシウムポンプの結晶構造解析
  • カイセツ キン ショウホウタイ カルシウム ポンプ ノ ケッショウ コウゾウ カイセキ

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Abstract

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.

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