title: Crystallization and preliminary X-ray characterization of a PaaX-like protein from Sulfolobus solfataricus P2.
abstract: 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.
authors: 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.
authors: Yi
authors: Y
authors: Cao
authors: Zhiyong
authors: Z
authors: Lou
authors: Yuna
authors: Y
authors: Sun
authors: Fei
authors: F
authors: Xue
authors: Changzeng
authors: C
authors: Feng
authors: Xiaocui
authors: X
authors: Gong
authors: Dongmei
authors: D
authors: Yang
authors: Mark
authors: M
authors: Bartlam
authors: Zhaohui
authors: Z
authors: Meng
authors: Keqin
authors: K
authors: Zhang
mesh_terms: 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*
chemical_list: D019843:Archaeal Proteins; D017931:DNA Primers