Crystallization and preliminary x-ray diffraction studies of Aes acetyl-esterase from Escherichia coli. (Articolo in rivista)

Type
Label
  • Crystallization and preliminary x-ray diffraction studies of Aes acetyl-esterase from Escherichia coli. (Articolo in rivista) (literal)
Anno
  • 2003-01-01T00:00:00+01:00 (literal)
Alternative label
  • Sorrentino N., De Simone G., Menchise V., Mandrich L., Rossi M., Manco G., Pedone C. (2003)
    Crystallization and preliminary x-ray diffraction studies of Aes acetyl-esterase from Escherichia coli.
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Sorrentino N., De Simone G., Menchise V., Mandrich L., Rossi M., Manco G., Pedone C. (literal)
Pagina inizio
  • 1846 (literal)
Pagina fine
  • 1848 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 59 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Titolo
  • Crystallization and preliminary x-ray diffraction studies of Aes acetyl-esterase from Escherichia coli. (literal)
Abstract
  • The acetyl-esterase Aes from Escherichia coli, which belongs to the HSL group of the esterase/lipase superfamily, has been crystallized by the hanging-drop vapour-diffusion method using polyethylene glycol 8000 as a precipitant and magnesium chloride as an additive. Crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 110.0, b = 190.6, c = 218.6 A. A complete data set has been collected to 2.5 A resolution at the Elettra synchrotron source, Trieste using a single frozen crystal. Packing density considerations agree with 10-16 monomers in the asymmetric unit, with a corresponding solvent content of 61-38%. (literal)
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