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

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)148-150
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume58
Issue number1
DOIs
Publication statusPublished - 2002 Feb 6
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology

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