Open AccessCrystallization and preliminary X‐ray analysis of CooA from Carboxydothermus hydrogenoformans
Author(s) -
Komori Hirofumi,
Satomoto Kensuke,
Ueda Yasufumi,
Shibata Naoki,
Inagaki Sayaka,
Yoshioka Shiro,
Aono Shigetoshi,
Higuchi Yoshiki
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106012826
Subject(s) - crystallization , materials science , chemistry , organic chemistry
CooA, a homodimeric haem‐containing protein, is responsible for transcriptional regulation in response to carbon monoxide (CO). It has a b‐type haem as a CO sensor. Upon binding CO to the haem, CooA binds promoter DNA and activates expression of genes for CO metabolism. CooA from Carboxydothermus hydrogenoformans has been overexpressed in Escherichia coli , purified and crystallized by the vapour‐diffusion method. The crystal belongs to space group P 2 1 , with unit‐cell parameters a = 61.8, b = 94.7, c = 92.8 Å, β = 104.8°. The native and anomalous difference Patterson maps indicated that two CooA dimers are contained in the asymmetric unit and are related by a translational symmetry almost parallel to the c axis.