Crystallization of scytalone dehydratase F162A mutant in the unligated state and a preliminary X-ray diffraction study at 37 K

Takayuki Motoyama, Masayoshi Nakasako, Isamu Yamaguchi

研究成果: Article

9 引用 (Scopus)

抜粋

Scytalone dehydratase variant F162A, in which Phe162 in the C-terminal region was replaced with alanine, was crystallized with polyethylene glycol 4000. Because the crystal was radiation-sensitive, the diffraction data were collected at cryogenic temperatures. The crystal belonged to monoclinic space group P21, with unit-cell parameters a = 72.64, b = 61.30, c = 72.62 Å, β = 120.02° at 37 K. The calculated VM value was acceptable when a trimer of the mutant enzyme occupied a crystallographic asymmetric unit. The resolution limit was extended to 1.45 Å at BL41XU of SPring-8 at 37 K.

元の言語English
ページ(範囲)148-150
ページ数3
ジャーナルActa Crystallographica Section D: Biological Crystallography
58
発行部数1
DOI
出版物ステータスPublished - 2002 2 6
外部発表Yes

ASJC Scopus subject areas

  • Structural Biology

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