Ann Arbor / Johannesburg / Horton / Victoria / P. Thermofluor / /
Company
Grishin N. V. / Protein Data Bank / Macmillan Publishers Limited. / Salomon / K. Metal / Ericsson / Honda / European Molecular Biology Laboratory / Roberts N. A. / Obayashi / J. / /
Country
France / United States / Vietnam / / /
Event
M&A / /
Facility
European Synchrotron Radiation Facility / PB1N complex / /
IndustryTerm
active site / metal ion mechanism / metal-free enzyme / cap-binding site / online version / endonuclease active site / divalent metal ions / active site metal binding / reaction products / metal-binding active sites / metal ions / metal ion binding sites / metal salts / metal / metal binding residues / structure similarity search / defined metal structure / weaker site / protein solution / metal-bound form / actual endonuclease active site / important divalent metal ion binding acidic residues / conserved core active site / metal sites / /
Movie
A.D. / /
Organization
Unit of Virus Host-Cell Interactions / European Union / INTERPOL / /
Person
Thibaut Cre / Chung / /
Position
T. D. / Butcher / R.W.H.R. Author Information Atomic coordinates / D.J. / Author / viral messenger / representative / /
Product
Nikon D90 Digital Camera / /
ProvinceOrState
Victoria / Pennsylvania / South Carolina / North Carolina / /
doi:[removed]nature07745 LETTERS The cap-snatching endonuclease of influenza virus polymerase resides in the PA subunit Alexandre Dias1*, Denis Bouvier1*, Thibaut Cre´pin1*, Andrew A. McCarthy1,2, Darren J. Hart1,2, Flo