Article
Structural basis for the influence of a single mutation K145N on the oligomerization and photoswitching rate of Dronpa.
Acta crystallographica. Section D, Biological crystallography - 1 Dec 2012
Nguyen Bich Ngan, Moeyaert Benjamien, Van Hecke Kristof, Dedecker Peter, Mizuno Hideaki, Hofkens Johan, Van Meervelt Luc
Abstract excerpt
The crystal structure of the on-state of PDM1-4, a single-mutation variant of the photochromic fluorescent protein Dronpa, is reported at 1.95 Å resolution. PDM1-4 is a Dronpa variant that possesses a slower off-switching rate than Dronpa and thus can effectively increase the image resolution in subdiffraction optical microscopy, although the precise molecular basis for this change has not been elucidated. This...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.
