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
Externally publishedYes

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scytalone dehydratase
Crystallization
X-Ray Diffraction
Alanine
Radiation
crystallization
X ray diffraction
Crystals
Temperature
alanine
Enzymes
cryogenic temperature
trimers
diffraction
Cryogenics
crystals
enzymes
glycols
polyethylenes
x rays

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics
  • Condensed Matter Physics
  • Structural Biology

Cite this

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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 {\AA}, 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 {\AA} at BL41XU of SPring-8 at 37 K.",
author = "Takayuki Motoyama and Masayoshi Nakasako and Isamu Yamaguchi",
year = "2002",
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T1 - Crystallization of scytalone dehydratase F162A mutant in the unligated state and a preliminary X-ray diffraction study at 37 K

AU - Motoyama, Takayuki

AU - Nakasako, Masayoshi

AU - Yamaguchi, Isamu

PY - 2002

Y1 - 2002

N2 - 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.

AB - 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.

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