Zobrazeno 1 - 10
of 50
pro vyhledávání: '"Frédéric Poitevin"'
Publikováno v:
Frontiers in Molecular Biosciences, Vol 11 (2024)
Molecules are essential building blocks of life and their different conformations (i.e., shapes) crucially determine the functional role that they play in living organisms. Cryogenic Electron Microscopy (cryo-EM) allows for acquisition of large image
Externí odkaz:
https://doaj.org/article/19a2396eda624f80a89cae989873551e
Publikováno v:
AIMS Mathematics, Vol 7, Iss 1, Pp 986-999 (2022)
Cryogenic electron microscopy (cryo-EM) has become widely used for the past few years in structural biology, to collect single images of macromolecules "frozen in time". As this technique facilitates the identification of multiple conformational stat
Externí odkaz:
https://doaj.org/article/8ecf21c9691d4844a0df44dea01c2a14
Autor:
Zhen Su, Medhanjali Dasgupta, Frédéric Poitevin, Irimpan I. Mathews, Henry van den Bedem, Michael E. Wall, Chun Hong Yoon, Mark A. Wilson
Publikováno v:
Structural Dynamics, Vol 8, Iss 4, Pp 044701-044701-18 (2021)
Protein structure and dynamics can be probed using x-ray crystallography. Whereas the Bragg peaks are only sensitive to the average unit-cell electron density, the signal between the Bragg peaks—diffuse scattering—is sensitive to spatial correlat
Externí odkaz:
https://doaj.org/article/83899f132e8540bdb34658d93de4e3e7
Publikováno v:
IUCrJ, Vol 5, Iss 2, Pp 211-222 (2018)
Conformational changes drive protein function, including catalysis, allostery and signaling. X-ray diffuse scattering from protein crystals has frequently been cited as a probe of these correlated motions, with significant potential to advance our un
Externí odkaz:
https://doaj.org/article/738ddd1f108c4edeb3e5faf8d021283e
Publikováno v:
Molecules, Vol 25, Iss 18, p 4262 (2020)
The extent of ribosomal heterogeneity has caught increasing interest over the past few years, as recent studies have highlighted the presence of structural variations of the ribosome. More precisely, the heterogeneity of the ribosome covers multiple
Externí odkaz:
https://doaj.org/article/50479058aee0454987bbfd93c6342528
Autor:
Ariana Peck, Hsing-Yin Chang, Antoine Dujardin, Deeban Ramalingam, Monarin Uervirojnangkoorn, Zhaoyou Wang, Adrian Mancuso, Frédéric Poitevin, Chun Hong Yoon
Publikováno v:
Journal of Applied Crystallography. 55:1002-1010
X-ray free electron lasers (XFEL) have the ability to produce ultra-bright femtosecond X-ray pulses for coherent diffraction imaging of biomolecules. While the development of methods and algorithms for macromolecular crystallography is now mature, XF
Autor:
Elyse A. Schriber, Daniel W. Paley, Robert Bolotovsky, Daniel J. Rosenberg, Raymond G. Sierra, Andrew Aquila, Derek Mendez, Frédéric Poitevin, Johannes P. Blaschke, Asmit Bhowmick, Ryan P. Kelly, Mark Hunter, Brandon Hayes, Derek C. Popple, Matthew Yeung, Carina Pareja-Rivera, Stella Lisova, Kensuke Tono, Michihiro Sugahara, Shigeki Owada, Tevye Kuykendall, Kaiyuan Yao, P. James Schuck, Diego Solis-Ibarra, Nicholas K. Sauter, Aaron S. Brewster, J. Nathan Hohman
Publikováno v:
Nature, vol 601, iss 7893
Nature
Nature
Inorganic–organic hybrid materials represent a large share of newly reported structures, owing to their simple synthetic routes and customizable properties1. This proliferation has led to a characterization bottleneck: many hybrid materials are obl
Publikováno v:
AIMS Mathematics, Vol 7, Iss 1, Pp 986-999 (2022)
Cryogenic electron microscopy (cryo-EM) has become widely used for the past few years in structural biology, to collect single images of macromolecules "frozen in time". As this technique facilitates the identification of multiple conformational stat
Autor:
Axel Levy, Frédéric Poitevin, Julien Martel, Youssef Nashed, Ariana Peck, Nina Miolane, Daniel Ratner, Mike Dunne, Gordon Wetzstein
Publikováno v:
Lecture Notes in Computer Science ISBN: 9783031198021
Comput Vis ECCV
Comput Vis ECCV
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:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e87dc567597f5bf11351f2f136d7718
https://doi.org/10.1007/978-3-031-19803-8_32
https://doi.org/10.1007/978-3-031-19803-8_32
Publikováno v:
Journal of Structural Biology. 214:107920
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