About: Crystallization and functional studies of trimeric lectin RS20L from bacterium Ralstonia solanacearum     Goto   Sponge   NotDistinct   Permalink

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Description
  • Extraordinary protein RS20L from R. solanacearum was chosen for multiple structural and functional studies. Oligomerization status and stability were tested. Isothermal titration calorimetry experiments confirmed binding to mannosylated dendrimers.
  • Extraordinary protein RS20L from R. solanacearum was chosen for multiple structural and functional studies. Oligomerization status and stability were tested. Isothermal titration calorimetry experiments confirmed binding to mannosylated dendrimers. (en)
Title
  • Crystallization and functional studies of trimeric lectin RS20L from bacterium Ralstonia solanacearum
  • Crystallization and functional studies of trimeric lectin RS20L from bacterium Ralstonia solanacearum (en)
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  • Crystallization and functional studies of trimeric lectin RS20L from bacterium Ralstonia solanacearum
  • Crystallization and functional studies of trimeric lectin RS20L from bacterium Ralstonia solanacearum (en)
skos:notation
  • RIV/00216224:14740/14:00078426!RIV15-MSM-14740___
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  • RIV/00216224:14740/14:00078426
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  • Ralstonia; MBP; lectin; trimer; protein purification; analytical ultracentrifugation; isothermal titration calorimetry; protein crystallization; SDS-PAGE (en)
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  • Komárek, Jan
  • Kostlánová, Nikola
  • Wimmerová, Michaela
  • Šulák, Ondřej
  • Kyseľ, Peter
http://localhost/t...ganizacniJednotka
  • 14740
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