Crystallization and preliminary X-ray diffraction studies of hyperthermostable glutamate dehydrogenase from Thermococcus profundus

Sadaharu Higuchi, Masayoshi Nakasako, Toshiaki Kudo

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Recombinant glutamate dehydrogenase from a hyperthermophilic archaeon. Thermococcus profundus, was crystallized in the presence of both polyethylene glycol 8000 and lithium sulfate. Four types of crystals having different morphologies appeared in the crystallization trials; however, only one type was suitable for X-ray crystal structure analysis. The crystal belonged to the monoclinic space group P21 and the unit-cell parameters were a = 112.99, b = 163.70, c = 133.07 Å, β = 113.46°at 110 K. The calculated V(M) value of 3.42 Å3 Da-1 was acceptable when one hexamer of the enzyme, which was the physiological functional unit, occupied a crystallographic asymmetric unit. X-ray diffraction intensity data were collected to a resolution of 2.25 Å with good statistics at the BL44B2 beamline of SPring-8.

Original languageEnglish
Pages (from-to)1917-1919
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume55
Issue number11
DOIs
Publication statusPublished - 1999 Nov
Externally publishedYes

Fingerprint

Thermococcus
Glutamate Dehydrogenase
glutamates
dehydrogenases
Archaea
Crystallization
X-Ray Diffraction
X-Rays
lithium sulfates
crystallization
X ray diffraction
Crystals
Enzymes
diffraction
crystals
enzymes
glycols
polyethylenes
x rays
Crystal structure

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 = "Recombinant glutamate dehydrogenase from a hyperthermophilic archaeon. Thermococcus profundus, was crystallized in the presence of both polyethylene glycol 8000 and lithium sulfate. Four types of crystals having different morphologies appeared in the crystallization trials; however, only one type was suitable for X-ray crystal structure analysis. The crystal belonged to the monoclinic space group P21 and the unit-cell parameters were a = 112.99, b = 163.70, c = 133.07 {\AA}, β = 113.46°at 110 K. The calculated V(M) value of 3.42 {\AA}3 Da-1 was acceptable when one hexamer of the enzyme, which was the physiological functional unit, occupied a crystallographic asymmetric unit. X-ray diffraction intensity data were collected to a resolution of 2.25 {\AA} with good statistics at the BL44B2 beamline of SPring-8.",
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AU - Higuchi, Sadaharu

AU - Nakasako, Masayoshi

AU - Kudo, Toshiaki

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AB - Recombinant glutamate dehydrogenase from a hyperthermophilic archaeon. Thermococcus profundus, was crystallized in the presence of both polyethylene glycol 8000 and lithium sulfate. Four types of crystals having different morphologies appeared in the crystallization trials; however, only one type was suitable for X-ray crystal structure analysis. The crystal belonged to the monoclinic space group P21 and the unit-cell parameters were a = 112.99, b = 163.70, c = 133.07 Å, β = 113.46°at 110 K. The calculated V(M) value of 3.42 Å3 Da-1 was acceptable when one hexamer of the enzyme, which was the physiological functional unit, occupied a crystallographic asymmetric unit. X-ray diffraction intensity data were collected to a resolution of 2.25 Å with good statistics at the BL44B2 beamline of SPring-8.

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