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Article citations


K. Onuma, A. Watanabe, N. Kanzaki and T. Kubota, “Association Kinetics of Wild-And Mutant-Type Ynd1p in Relation to Quality of Grown Crystals,” Journal of Physical Chemistry B, Vol. 110, No. 49, 2006, pp. 24876- 24883.

has been cited by the following article:

  • TITLE: Crystallization of Cellobiohydrolase in the Presence of Cellulose-Degraded Cellobiose: Analysis of Intermolecular Interactions and Association Dynamics

    AUTHORS: Kazuo Onuma, Naoki Furubayashi, Fujiko Shibata, Yoshiko Kobayashi, Sachiko Kaito, Yuki Ohnishi, Koji Inaka

    KEYWORDS: Enzyme Crystallization; Inhibitor; Hamaker Constant; Light Scattering

    JOURNAL NAME: Journal of Crystallization Process and Technology, Vol.4 No.1, January 2, 2014

    ABSTRACT: Crystallization of enzymes in presence of impurities is important for clarifying the role of enzymes in natural world. Although it is proposed that impurities inhibit nucleation of enzyme crystallization, details are unclear. In this study, crystallization of cellobiohydrolase from Aspergillus niger was investigated by dynamic and time-resolved static light scattering using cellobiose as an impurity. We aimed to clarify how cellobiose inhibits cellobiohydrolase crystallization and to crystallize cellobiohydrolase in concentrated cellobiose without using seeds. The contribution of attractive forces to total intermolecular interactions of cellobiohydrolase monomers increased with the molar ratio of cellobiose/cellobiohydrolase (R(cb/ce)). Association dynamics of cellobiohydrolase using lithium sulfate, however, showed that the initial aggregation rate decreased with an increase in R(cb/ce). Because binding sites of cellobioses to cellobiohydrolase molecules differed from those for the growth of protein crystals, the binding of cellobioses would increase the chemical potential of the cellobiohydrolase monomers, which gradually reduced supersaturation for growth as the aggregate size increased. This result was in contrast with the conventional idea that cellobiose inhibits the nucleation of cellobiohydrolase crystals. Gentle agitation of cellobiose-containing cellobiohydrolase solutions during sitting-drop vapor-diffusion growth resulted in the growth of cellobiohydrolase single crystals for all R(cb/ce) conditions without using seeds.