1 results match your criteria: "USA and Children's Hospital of Philadelphia Research Institute[Affiliation]"
Quaternary arrangement of an active, native group II intron ribonucleoprotein complex revealed by small-angle X-ray scattering.
Nucleic Acids Res
April 2014
Department of Biochemistry & Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104-6059, USA, Department of Chemical Engineering, University of Texas at Austin, Austin, TX 78712, USA, Wadsworth Center, NYS Department of Health, Albany, NY 12201, USA, Department of Biological Sciences and RNA Institute, University at Albany, State University of New York, Albany, NY 12222, USA, SUNY Downstate Medical Center, University Hospital, Brooklyn, NY 11203, USA and Children's Hospital of Philadelphia Research Institute, Philadelphia, PA 19104, USA.
The stable ribonucleoprotein (RNP) complex formed between the Lactococcus lactis group II intron and its self-encoded LtrA protein is essential for the intron's genetic mobility. In this study, we report the biochemical, compositional, hydrodynamic and structural properties of active group II intron RNP particles (+A) isolated from its native host using a novel purification scheme. We employed small-angle X-ray scattering to determine the structural properties of these particles as they exist in solution.
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