Zobrazeno 1 - 10
of 122
pro vyhledávání: '"Poitevin Frederic"'
Autor:
Thayer Jana, Chen Zhantao, Claus Richard, Damiani Daniel, Ford Christopher, Dubrovin Mikhail, Elmir Victor, Kroeger Wilko, Li Xiang, Marchesini Stefano, Mariani Valerio, Melcchiori Riccardo, Nelson Silke, Peck Ariana, Perazzo Amedeo, Poitevin Frederic, O’Grady Christopher Paul, Otero Julieth, Quijano Omar, Shankar Murali, Uervirojnangkoorn Monarin, Veraldi Riccardo, Weaver Matthew, Weninger Clemens, Yamajala Seshu, Wang Cong, Yoon Chun Hong
Publikováno v:
EPJ Web of Conferences, Vol 295, p 13002 (2024)
The increasing volumes of data produced at light sources such as the Linac Coherent Light Source (LCLS) enable the direct observation of materials and molecular assemblies at the length and timescales of molecular and atomic motion. This exponential
Externí odkaz:
https://doaj.org/article/cc8c7579faa446e98839e02c9c6cf13c
Autor:
Levy, Axel, Chan, Eric R., Fridovich-Keil, Sara, Poitevin, Frédéric, Zhong, Ellen D., Wetzstein, Gordon
The interaction of a protein with its environment can be understood and controlled via its 3D structure. Experimental methods for protein structure determination, such as X-ray crystallography or cryogenic electron microscopy, shed light on biologica
Externí odkaz:
http://arxiv.org/abs/2406.04239
X-ray free-electron lasers (XFELs) offer unique capabilities for measuring the structure and dynamics of biomolecules, helping us understand the basic building blocks of life. Notably, high-repetition-rate XFELs enable single particle imaging (X-ray
Externí odkaz:
http://arxiv.org/abs/2312.14432
Single neurons in neural networks are often interpretable in that they represent individual, intuitively meaningful features. However, many neurons exhibit $\textit{mixed selectivity}$, i.e., they represent multiple unrelated features. A recent hypot
Externí odkaz:
http://arxiv.org/abs/2310.11431
Cryogenic electron microscopy (cryo-EM) has transformed structural biology by allowing to reconstruct 3D biomolecular structures up to near-atomic resolution. However, the 3D reconstruction process remains challenging, as the 3D structures may exhibi
Externí odkaz:
http://arxiv.org/abs/2306.07274
Publikováno v:
Neural Information Processing Systems (NeurIPS) 2022
Cryo-electron microscopy (cryo-EM) is an imaging modality that provides unique insights into the dynamics of proteins and other building blocks of life. The algorithmic challenge of jointly estimating the poses, 3D structure, and conformational heter
Externí odkaz:
http://arxiv.org/abs/2210.07387
Autor:
Nashed, Youssef, Peck, Ariana, Martel, Julien, Levy, Axel, Koo, Bongjin, Wetzstein, Gordon, Miolane, Nina, Ratner, Daniel, Poitevin, Frédéric
Cryogenic electron microscopy (cryo-EM) provides a unique opportunity to study the structural heterogeneity of biomolecules. Being able to explain this heterogeneity with atomic models would help our understanding of their functional mechanisms but t
Externí odkaz:
http://arxiv.org/abs/2209.15121
Autor:
Levy, Axel, Poitevin, Frédéric, Martel, Julien, Nashed, Youssef, Peck, Ariana, Miolane, Nina, Ratner, Daniel, Dunne, Mike, Wetzstein, Gordon
Cryo-electron microscopy (cryo-EM) has become a tool of fundamental importance in structural biology, helping us understand the basic building blocks of life. The algorithmic challenge of cryo-EM is to jointly estimate the unknown 3D poses and the 3D
Externí odkaz:
http://arxiv.org/abs/2203.08138
Recent breakthroughs in high-resolution imaging of biomolecules in solution with cryo-electron microscopy (cryo-EM) have unlocked new doors for the reconstruction of molecular volumes, thereby promising further advances in biology, chemistry, and pha
Externí odkaz:
http://arxiv.org/abs/2201.02867
Publikováno v:
In Current Opinion in Structural Biology June 2024 86