Shape of α-crystallin analyzed by small-angle neutron scattering

Masaaki Sugiyama, Noriko Fujii, Yukio Morimoto, Toshiya Otomo, Shinichi Takata, Masakatsu Misawa, Masahiko Annaka, Keiji Itoh, Kazuhiro Mori, Takashi Sato, Sakie Kurabayashi, Toshiharu Fukunaga

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)


The size and shape of aggregates of human recombinant αA-crystallin and αB-crystallin are investigated with small-angle neutron scattering and dynamic light scattering. At a bioactive temperature (310 K), both polypeptides form aggregates with almost the same size and shape. The αB-crystallin maintains an almost identical size and shape at 310 and 288 K, whereas the aggregate of αA-crystallin shows deformation at 288 K. This result suggests that at the lower temperature there is a difference in structural stability between the two aggregates of the polypeptides.

Original languageEnglish
Pages (from-to)s200-s204
JournalJournal of Applied Crystallography
Issue numberSUPPL. 1
Publication statusPublished - Apr 2007

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)


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