Crystallization and preliminary X-ray characterization of a PaaX-like protein from Sulfolobus solfataricus P2.
PaaX is a global regulator of the phenylacetyl-coenzyme A catabolon that adjusts the expression of different operons to that of the paa-encoded central pathway. In this study, the PaaX-like protein from the hyperthermophilic archaeon Sulfolobus solfataricus P2 was successfully crystallized by the hanging-drop vapour-diffusion method using ammonium sulfate as a precipitant. Diffraction data were obtained to a resolution of 3.0 A using synchrotron radiation at the Photon Factory. The crystal belonged to space group P321, with unit-cell parameters a = 86.4, b = 86.4, c = 105.5 A.
Cao
Yi
Y
Laboratory for Conservation and Utilization of Bio-Resources and Key Laboratory for Microbial Resources of the Ministry of Education, Yunnan University, Kunming, Yunnan 650091, People's Republic of China.
Lou
Zhiyong
Z
Sun
Yuna
Y
Xue
Fei
F
Feng
Changzeng
C
Gong
Xiaocui
X
Yang
Dongmei
D
Bartlam
Mark
M
Meng
Zhaohui
Z
Zhang
Keqin
K
D019843:Archaeal Proteins / Q000737:chemistry*; D001483:Base Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D017931:DNA Primers; D016133:Polymerase Chain Reaction; D011487:Protein Conformation; D048229:Sulfolobus solfataricus / Q000737:chemistry*
D019843:Archaeal Proteins; D017931:DNA Primers