日本結晶学会誌
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52 巻 , 1 号
選択された号の論文の26件中1~26を表示しています
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特集 構造生物学研究の新展開
1.タンパク質構造研究に対する結晶学の役割
  • 月原 冨武, 田之倉 優, 三木 邦夫
    52 巻 (2010) 1 号 p. 2
    公開日: 2011/02/25
    ジャーナル フリー
  • 月原 冨武
    52 巻 (2010) 1 号 p. 3-7
    公開日: 2011/02/25
    ジャーナル フリー
    Structural studies on membrane proteins have been performed at atomic level by both three-dimensional X-ray crystallography and two-dimensional electron crystallography in Japan as in Europe and Unites States. More than 13 membrane protein structures were elucidate by X-ray method in our country, and seven membrane protein structures were determined by cryo-electron microscopic method developed by Fujiyoshi of Kyoto University. Extensive crystallographic studies on calcium pump and cytochrome c oxidase elucidated their functional mechanisms at atomic level.
    Structure and switching mechanism of a flagellum were studied by X-ray and electron microscopic methods. Vault structure exhibiting D39 symmetry was determined by X-ray method.
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  • 田之倉 優, 永田 宏次, 宮園 健一, 宮川 拓也, 岡井 公彦
    52 巻 (2010) 1 号 p. 8-13
    公開日: 2011/02/25
    ジャーナル フリー
    Structural biology has made tremendous progress in this decade. Here we briefly introduce the Target Proteins Research Program, a national project promoted by the Ministry of Education, Culture, Sports, Science and Technology (MEXT) of Japan. The program aims to reveal the structure and function of proteins that are of great importance in both academic research and industrial application. We also summarize the results of structure-function analyses of (i) transcriptional regulatory proteins useful for the breading of drought and heat stress tolerant crops, (ii) useful enzymes for the production of chiral compounds, and (iii) useful enzymes for the degradation of environmental pollution substances. These results can be utilized in various areas of industries, to enhance food production, to improve the efficiency of pharmaceutical compound production, and to promote the bioremediation of contaminated soil and water.
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  • 竹田 一旗, 平野 優, 三木 邦夫
    52 巻 (2010) 1 号 p. 14-18
    公開日: 2011/02/25
    ジャーナル フリー
    Many protein structures have been determined by X-ray crystallography and deposited with the Protein Data Bank. However, these structures at usual resolution (1.5<d<3.0 Å) are insufficient in their precision and quantity for elucidating the molecular mechanism of protein functions directly from structural information. Several studies at ultra-high resolution (d<0.8 Å) have been performed with synchrotron radiation in the last decade. The highest resolution of the protein crystals was achieved at 0.54 Å resolution for a small protein, crambin. In such high resolution crystals, almost all of hydrogen atoms of proteins and some hydrogen atoms of bound water molecules are experimentally observed. In addition, outer-shell electrons of proteins can be analyzed by the multipole refinement procedure. However, the influence of X-rays should be precisely estimated in order to derive meaningful information from the crystallographic results. In this review, we summarize refinement procedures, current status and perspectives for ultra high resolution protein crystallography.
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2.基礎研究から応用展開に向けて
(a)包括的構造生物学基礎研究
(b)技術開発型研究
(c)応用指向型研究
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