TY - JOUR
T1 - Crystallization and preliminary X-ray studies of an electron-transfer complex of ferredoxin and ferredoxin-dependent glutamate synthase from the cyanobacterium Leptolyngbya boryana
AU - Shinmura, Kanako
AU - Muraki, Norifumi
AU - Yoshida, Ayako
AU - Hase, Toshiharu
AU - Kurisu, Genji
PY - 2012/3
Y1 - 2012/3
N2 - 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.
AB - 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.
KW - electron-transfer complex
KW - ferredoxin
KW - glutamate synthase
UR - http://www.scopus.com/inward/record.url?scp=84858975914&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84858975914&partnerID=8YFLogxK
U2 - 10.1107/S1744309112003387
DO - 10.1107/S1744309112003387
M3 - Article
C2 - 22442234
AN - SCOPUS:84858975914
SN - 1744-3091
VL - 68
SP - 324
EP - 327
JO - Acta Crystallographica Section F:Structural Biology Communications
JF - Acta Crystallographica Section F:Structural Biology Communications
IS - 3
ER -