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Clinton S. Potter

Researcher at Columbia University

Publications -  197
Citations -  14143

Clinton S. Potter is an academic researcher from Columbia University. The author has contributed to research in topics: Computer science & Particle. The author has an hindex of 52, co-authored 178 publications receiving 11850 citations. Previous affiliations of Clinton S. Potter include University of Illinois at Urbana–Champaign & University of California, Santa Barbara.

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Automated molecular microscopy: the new Leginon system.

TL;DR: The primary automated data acquisition software system, Leginon, has been completely redesigned over the past two years and the system has demonstrated the capacity for high throughput data acquisition by acquiring images of more than 100,000 particles in a single session at the microscope.
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Appion: an integrated, database-driven pipeline to facilitate EM image processing.

TL;DR: The vision for this technique is to provide a straightforward manner in which users can proceed from raw data to a reliable 3D reconstruction through a pipeline that both facilitates management of the processing steps and makes the results at each step more transparent.
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Cryo-EM Structure of a Fully Glycosylated Soluble Cleaved HIV-1 Envelope Trimer

TL;DR: A cryo–electron microscopy reconstruction and structural model of a cleaved, soluble Env trimer in complex with a CD4 binding site bnAb, PGV04 is presented, which reveals the spatial arrangement of Env components, including the V1/V2, V3, HR1, and HR2 domains, as well as shielding glycans.
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Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser

Yanyong Kang, +71 more
- 30 Jul 2015 - 
TL;DR: The crystal structure of a constitutively active form of human rhodopsin bound to a pre-activated form of the mouse visual arrestin is determined by serial femtosecond X-ray laser crystallography and provides a basis for understanding GPCR-mediated arrestin-biased signalling.
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Addressing Preferred Specimen Orientation in Single-Particle Cryo-EM through Tilting

TL;DR: These methods were applied to determine the structures at near-atomic resolution of the influenza hemagglutinin trimer, which adopts a highly preferred specimen orientation, and of ribosomal biogenesis intermediates, which adopt moderately preferred orientations.