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

出版社

INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309112003387

关键词

ferredoxin; glutamate synthase; electron-transfer complex

资金

  1. Academia Sinica
  2. National Synchrotron Radiation Research Center (Taiwan)
  3. Ministry of Education, Culture, Sports, Science and Technology of Japan
  4. Funding Program for Next-Generation World-Leading Research
  5. Grants-in-Aid for Scientific Research [11J05122, 20370022] Funding Source: KAKEN

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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 angstrom resolution. The crystals belonged to space group P43, with unit-cell parameters a = b = 84.95, c = 476.31 angstrom.

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