Crystallization and preliminary X-ray structural studies of human prouroguanylin

Len Ito, Yuji Hidaka, Masaki Okumura, Hironori Konishi, Hiroshi Yamaguchi

研究成果: Article査読

5 被引用数 (Scopus)

抄録

Uroguanylin, which serves as an endogenous ligand of guanylyl cyclase C, is initially secreted in the form of a precursor, prouroguanylin. The N-terminal region of prouroguanylin interacts with the mature portion of prouroguanylin during the folding pathway. Here, a preliminary X-ray crystallographic study of prouroguanylin is presented. Prouroguanylin was refolded, purified and crystallized using the hanging-drop vapour-diffusion method. Prouroguanylin crystals were cryocooled and used for data collection. The diffraction data showed that the crystals belonged to space group P6122, with unit-cell parameters a = b = 55.6, c = 157.7 Å, and diffracted to 2.5 Å resolution. The structure is currently being analyzed.

本文言語English
ページ(範囲)531-532
ページ数2
ジャーナルActa Crystallographica Section F: Structural Biology and Crystallization Communications
64
6
DOI
出版ステータスPublished - 2008
外部発表はい

ASJC Scopus subject areas

  • 生物理学
  • 構造生物学
  • 生化学
  • 遺伝学
  • 凝縮系物理学

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