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 1
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology

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