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  • Fujiwara, Takaaki  (2)
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  • 1
    Online Resource
    Online Resource
    Elsevier BV ; 2013
    In:  Biochemical and Biophysical Research Communications Vol. 431, No. 4 ( 2013-02), p. 802-807
    In: Biochemical and Biophysical Research Communications, Elsevier BV, Vol. 431, No. 4 ( 2013-02), p. 802-807
    Type of Medium: Online Resource
    ISSN: 0006-291X
    RVK:
    Language: English
    Publisher: Elsevier BV
    Publication Date: 2013
    detail.hit.zdb_id: 1461396-7
    SSG: 12
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  • 2
    Online Resource
    Online Resource
    International Union of Crystallography (IUCr) ; 2014
    In:  Acta Crystallographica Section A Foundations and Advances Vol. 70, No. a1 ( 2014-08-05), p. C1159-C1159
    In: Acta Crystallographica Section A Foundations and Advances, International Union of Crystallography (IUCr), Vol. 70, No. a1 ( 2014-08-05), p. C1159-C1159
    Abstract: Recent progress in the techniques of bio-macromolecular crystallography makes crystal structure analysis more powerful and useful for life science. The structure analysis of huge super-molecular (eukaryotic Ribosome, Vault etc.) and membrane proteins related to diseases were successful. Moreover, the structure/fragment drug design using crystal structure analysis method is also becoming reliable. However, crystallization still remains as a major bottleneck for determining bio-macromolecular structures, although many methods have been developed such as crystallization kits, crystallization robot, crystallizing in gel, space, and magnetic field, laser excitation, using antibody, modification of protein surface, and so forth. The current situation of crystallization is still dependent on the accidental method searching for a crystallization reagent and the growth environment since the methodology for obtaining a quality crystal for structure analysis is not established yet. Therefore, further development of more advanced crystallization methods is required to increase the probability of successful crystallization. In principal, probability of successful crystallization could be increased by polymerized molecules with 2 or 3-fold rotation symmetry [1]. We have solved more than 100 structures, and found some fragments which is isolated from core structure, and seem to contribute to form high quality crystal by forming a polymer with 2 or 3-fold axial symmetry. Thus, we developed a novel method by fussing target protein with crystallization tags named 2/3RS-tag. These 2/3RS-tags polymerize target proteins with 2 or 3-fold axial symmetry, and consequently accelerate formation of crystal. We will report and discuss this new method in this presentation.
    Type of Medium: Online Resource
    ISSN: 2053-2733
    Language: Unknown
    Publisher: International Union of Crystallography (IUCr)
    Publication Date: 2014
    detail.hit.zdb_id: 2020844-3
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