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Zeiss Spinning Disk Microscopy Digital Video Gallery

Human Cervix Adenocarcinoma Cells with mRuby-Clathrin

Clathrin is a highly conserved protein initially isolated in the mid-1970s by British researcher Barbara Pearse. Chains of clathrin organize into triskelion form, with three branching legs radiating from a central point. Clathrin triskelions join together into lattices on the inside of sections of cell membrane termed coated pits early during the process of receptor-mediated endocytosis. Clathrin-coated vesicles are then produced via invagination of the coated pit.

The human cervix adenocarcinoma cells (the HeLa line) featured in this digital video sequence are shown expressing mRuby fused to clathrin. The red fluorescent protein mRuby is a derivative of eqFP611, an Anthozoan far-red fluorescent protein. mRuby displays a large Stokes shift, exhibiting excitation and emission maxima at 558 and 605 nanometers, respectively. Nearly 30 additional mutations separate mRuby from its parent protein.