B
Bridget Carragher
Researcher at Columbia University
Publications - 283
Citations - 18225
Bridget Carragher is an academic researcher from Columbia University. The author has contributed to research in topics: Particle & Workflow. The author has an hindex of 59, co-authored 262 publications receiving 15693 citations. Previous affiliations of Bridget Carragher include Scripps Research Institute & University of the Witwatersrand.
Papers
More filters
Journal ArticleDOI
Automated molecular microscopy: the new Leginon system.
Christian Suloway,James Pulokas,Denis Fellmann,Anchi Cheng,Francisco Guerra,Joel Quispe,Scott M. Stagg,Clinton S. Potter,Bridget Carragher +8 more
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.
Journal ArticleDOI
Appion: an integrated, database-driven pipeline to facilitate EM image processing.
Gabriel C. Lander,Scott M. Stagg,Neil R. Voss,Anchi Cheng,Denis Fellmann,James Pulokas,Craig Yoshioka,Christopher Irving,Anke M. Mulder,Pick-Wei Lau,Dmitry Lyumkis,Clinton S. Potter,Bridget Carragher +12 more
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.
Journal ArticleDOI
A structural change in the kinesin motor protein that drives motility
Sarah E. Rice,Abel W. Lin,Daniel Safer,Cynthia L. Hart,Nariman Naber,Bridget Carragher,Shane M. Cain,Elena Pechatnikova,Elizabeth M. Wilson-Kubalek,Michael Whittaker,Edward Pate,Roger Cooke,Edwin W. Taylor,Ronald A. Milligan,Ronald D. Vale +14 more
TL;DR: A large conformational change of a ∼15-amino-acid region (the neck linker) in kinesin is detected and visualized using electron paramagnetic resonance, fluorescence resonance energy transfer, pre-steady state kinetics and cryo-electron microscopy.
Journal ArticleDOI
Cryo-EM Structure of a Fully Glycosylated Soluble Cleaved HIV-1 Envelope Trimer
Dmitry Lyumkis,Jean-Philippe Julien,Natalia de Val,Albert Cupo,Clinton S. Potter,Per Johan Klasse,Dennis R. Burton,Rogier W. Sanders,Rogier W. Sanders,John P. Moore,Bridget Carragher,Ian A. Wilson,Andrew B. Ward,Andrew B. Ward +13 more
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.
Journal ArticleDOI
Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser
Yanyong Kang,X. Edward Zhou,Xiang Gao,Yuanzheng He,Wei Liu,Andrii Ishchenko,Anton Barty,Thomas A. White,Oleksandr Yefanov,Gye Won Han,Qingping Xu,Parker W. de Waal,Jiyuan Ke,M. H. Eileen Tan,Chenghai Zhang,Arne Moeller,Graham M. West,Bruce D. Pascal,Ned Van Eps,Lydia N. Caro,Sergey A. Vishnivetskiy,Regina J. Lee,Kelly Suino-Powell,Xin Gu,Kuntal Pal,Jinming Ma,Xiaoyong Zhi,Sébastien Boutet,Garth J. Williams,Marc Messerschmidt,Cornelius Gati,Nadia A. Zatsepin,Dingjie Wang,Daniel James,Shibom Basu,Shatabdi Roy-Chowdhury,Chelsie E. Conrad,Jesse Coe,Haiguang Liu,Stella Lisova,Christopher Kupitz,Ingo Grotjohann,Raimund Fromme,Yi Jiang,Minjia Tan,Huaiyu Yang,Jun Li,Meitian Wang,Zhong Zheng,Dianfan Li,Nicole Howe,Yingming Zhao,Jörg Standfuss,Kay Diederichs,Yuhui Dong,Clinton S. Potter,Bridget Carragher,Martin Caffrey,Hualiang Jiang,Henry N. Chapman,John C. H. Spence,Petra Fromme,Uwe Weierstall,Oliver P. Ernst,Vsevolod Katritch,Vsevolod V. Gurevich,Patrick R. Griffin,Wayne L. Hubbell,Raymond C. Stevens,Vadim Cherezov,Karsten Melcher,H. Eric Xu +71 more
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.