ArticleActa crystallographica. Section F, Structural biology and crystallization communications2009
Crystallization and preliminary X-ray characterization of a PaaX-like protein from Sulfolobus solfataricus P2.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed.
- Microbial degradation of aromatic compounds - from one strategy to four.Nature reviews. Microbiology · 2011Review
- Crystallization and preliminary X-ray diffraction studies of the transcriptional repressor PaaX, the main regulator of the phenylacetic acid degradation pathway in Escherichia coli W.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
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10 authors.
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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.
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