Design, construction, crystallization, and preliminary X-ray studies of a fine-tuning mutant (F133V) of module-substituted chimera hemoglobin

Tsuyoshi Shirai, Masahiro Fujikake, Takashi Yamane, Kenji Inaba, Koichiro Ishimori, Isao Morishima

研究成果: Article査読

2 被引用数 (Scopus)

抄録

A chimera βα-subunit of human hemoglobin was crystallized into a carbonmonoxy form. The protein was assembled by substituting the structural portion of a β-subunit of hemoglobin (M4 module of the subunit) for its counterpart in the α-subunit. In order to overcome the inherent instability in the crystallization of the chimera subunit, a site-directed mutagenesis (F133V) technique was employed based on a computer model. The crystal was used for an X-ray diffraction study yielding a data set with a resolution of 2.5 Å. The crystal belongs to the monoclinic space group P21, with cell dimensions of a = 62.9, b = 81.3, c = 55.1 Å, and β = 91.0°. These dimensions are similar to the crystallographic parameters of the native β- subunit tetramers in three different ligand states, one of which is a cyanide form that was also crystallized in this study.

本文言語English
ページ(範囲)263-267
ページ数5
ジャーナルProteins: Structure, Function and Genetics
32
3
DOI
出版ステータスPublished - 1998 8月 15
外部発表はい

ASJC Scopus subject areas

  • 構造生物学
  • 生化学
  • 分子生物学

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