Crystallization and preliminary X-ray studies of an electron-transfer complex of ferredoxin and ferredoxin-dependent glutamate synthase from the cyanobacterium Leptolyngbya boryana

Kanako Shinmura, Norifumi Muraki, Ayako Yoshida, Toshiharu Hase, Genji Kurisu

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)

Abstract

Ferredoxin (Fd) dependent glutamate synthase (Fd-GOGAT) is a key enzyme involved in nitrogen assimilation that catalyzes the two-electron reductive conversion of Gln and 2-oxoglutarate to two molecules of Glu. Fd serves as an electron donor for Fd-GOGAT and the two proteins form a transient electron-transfer complex. In this study, these two proteins were cocrystallized using the hanging-drop vapour-diffusion method. Diffraction data were collected and processed at 2.65 Å resolution. The crystals belonged to space group P43, with unit-cell parameters a = b = 84.95, c = 476.31 Å.

Original languageEnglish
Pages (from-to)324-327
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume68
Issue number3
DOIs
Publication statusPublished - 2012 Mar
Externally publishedYes

Keywords

  • electron-transfer complex
  • ferredoxin
  • glutamate synthase

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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