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Crystallization and preliminary X-ray characterization of a PaaX-like protein fromSulfolobus solfataricusP2

Authors :
Zhaohui Meng
Changzeng Feng
Dongmei Yang
Yuna Sun
Yi Cao
Zhiyong Lou
Ke-Qin Zhang
Mark Bartlam
Fei Xue
Xiaocui Gong
Source :
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 65:776-778
Publication Year :
2009
Publisher :
International Union of Crystallography (IUCr), 2009.

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.

Details

ISSN :
17443091
Volume :
65
Database :
OpenAIRE
Journal :
Acta Crystallographica Section F Structural Biology and Crystallization Communications
Accession number :
edsair.doi.dedup.....a7263a0d26969349c10badeab84bd7df