Crystallization and Preliminary X-ray Studies of an Electron-transfer Complex of Ferredoxin and Ferredoxin-dependent Glutamate Synthase from the Cyanobacterium Leptolyngbya Boryana

Overview

Journal Acta Crystallogr Sect F Struct Biol Cryst Commun

Date 2012 Mar 24

PMID 22442234

Citations 2

Authors

Kanako Shinmura

Norifumi Muraki

Ayako Yoshida

Toshiharu Hase

Genji Kurisu

Affiliations

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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 P4(3), with unit-cell parameters a = b = 84.95, c = 476.31 Å.

Citing Articles

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