Open AccessCrystallization and preliminary X‐ray diffraction studies of hyperthermophilic archaeal Rieske‐type ferredoxin (ARF) from Sulfolobus solfataricus P1
Author(s) -
Kounosu Asako,
Hasegawa Kazuya,
Iwasaki Toshio,
Kumasaka Takashi
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110019263
Subject(s) - sulfolobus solfataricus , ferredoxin , ammonium sulfate , crystallography , crystallization , chemistry , escherichia coli , archaea , biochemistry , chromatography , enzyme , organic chemistry , gene
The hyperthermophilic archaeal Rieske‐type [2Fe–2S] ferredoxin (ARF) from Sulfolobus solfataricus P1 contains a low‐potential Rieske‐type [2Fe–2S] cluster that has served as a tractable model for ligand‐substitution studies on this protein family. Recombinant ARF harbouring a pET30a vector‐derived N‐terminal extension region plus a hexahistidine tag has been heterologously overproduced in Escherichia coli , purified and crystallized by the hanging‐drop vapour‐diffusion method using 0.05 M sodium acetate, 0.05 M HEPES, 2 M ammonium sulfate pH 5.5. The crystals diffracted to 1.85 Å resolution and belonged to the tetragonal space group P 4 3 2 1 2, with unit‐cell parameters a = 60.72, c = 83.31 Å. The asymmetric unit contains one protein molecule.