Zobrazeno 1 - 10 of 15 568 pro vyhledávání: '"CRYOMICROSCOPY"'
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Akademický článek
High-resolution electron cryomicroscopy of V-ATPase in native synaptic vesicles.
Autor: Coupland, Claire E.1, Karimi, Ryan1,2, Bueler, Stephanie A.1, Yingke Liang1,3, Courbon, Gautier M.1,2, Trani, Justin M. Di1, Wong, Cassandra J.4, Saghian, Rayan5,6, Ji-Young Youn7,8,9, Lu-Yang Wang10,11, Rubinstein, John L.1,2,3 john.rubinstein@utoronto.ca
Publikováno v: Science. 7/12/2024, Vol. 385 Issue 6705, p168-174. 7p. 1 Color Photograph, 3 Diagrams.
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2
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Estimating the tails of the spectrum of the Hessian of the log-likelihood for \textit{ab-initio} single-particle reconstruction in electron cryomicroscopy
Autor: Rangan, Aaditya V., Tang, Wai-Shing, Cossio, Pilar, Zhang, Kexin, Grigorieff, Nikolaus
Electron cryomicroscopy (cryo-EM) is a technique in structural biology used to reconstruct accurate volumetric maps of molecules. One step of the cryo-EM pipeline involves solving an inverse-problem. This inverse-problem, referred to as \textit{ab-in
Externí odkaz: http://arxiv.org/abs/2411.13263
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3
Akademický článek
Structure of the Pseudomonas aeruginosa PAO1 Type IV pilus.
Autor: Ochner, Hannah1 (AUTHOR), Böhning, Jan1 (AUTHOR), Wang, Zhexin1 (AUTHOR), Tarafder, Abul K.1 (AUTHOR), Caspy, Ido1 (AUTHOR), Bharat, Tanmay A. M.1 (AUTHOR) tbharat@mrc-lmb.cam.ac.uk
Publikováno v: PLoS Pathogens. 12/12/2024, Vol. 20 Issue 12, p1-19. 19p.
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4
Akademický článek
Open‐source hardware‐ and software‐based cryomicroscopy system for investigation of phase transitions in cryobiological research.
Autor: Pakhomov, Oleksandr1 (AUTHOR) aleksandr.pakhomov2017@gmail.com, Shevchenko, Nadiia1 (AUTHOR), Chernobai, Nadiia1 (AUTHOR), Prokopiuk, Volodymyr1 (AUTHOR), Yershov, Serhii1 (AUTHOR), Bozhok, Galyna1 (AUTHOR)
Publikováno v: Journal of Microscopy. Feb2024, Vol. 293 Issue 2, p71-85. 15p.
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5
Akademický článek
"Seeing Is Believing": How Neutron Crystallography Informs Enzyme Mechanisms by Visualizing Unique Water Species hydrogen is the lightest atom and composes approximately half of the atomic content in macromolecules, yet their location can only be inferred or predicted in most macromolecular structures. This is because hydrogen can rarely be directly observed by the most common structure determination techniques (such as X-ray crystallography and electron cryomicroscopy). However, knowledge of hydrogen atom positions, especially for enzymes, can reveal protonation states of titratable active site residues, hydrogen bonding patterns, and the orientation of water molecules. Though we know they are present, this vital layer of information, which can inform a myriad of biological processes, is frustratingly invisible to us. The good news is that, even at modest resolution, neutron crystallography (NC) can reveal this layer and has emerged this century as a powerful tool to elucidate enzyme catalytic mechanisms. Due to its strong and coherent scattering of neutrons, incorporation of deuterium into the protein crystal amplifies the power of NC. This is especially true when solvation and the specific participation of key water molecules are crucial for catalysis. Neutron data allow the modeling of all three atoms in water molecules and have even revealed previously unobserved and unique species such as hydronium (D3O+) and deuteroxide (OD−) ions as well as lone deuterons (D+). Herein, we briefly review why neutrons are ideal probes for identifying catalytically important water molecules and these unique water-like species, limitations in interpretation, and four vignettes of enzyme success stories from disparate research groups. One of these groups was that of Dr. Chris G. Dealwis, who died unexpectedly in 2022. As a memorial appreciation of his scientific career, we will also highlight his interest and contributions to the
Autor: Wan, Qun1 (AUTHOR) qunwan@njau.edu.cn, Bennett, Brad C.2 (AUTHOR) qunwan@njau.edu.cn
Publikováno v: Biology (2079-7737). Nov2024, Vol. 13 Issue 11, p850. 15p.
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6
Akademický článek
Wilson statistics: derivation, generalization and applications to electron cryomicroscopy.
Publikováno v: Acta Crystallographica. Section A, Foundations & Advances. Sep2021, Vol. 77 Issue 5, p472-479. 8p.
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7
Akademický článek
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9
Akademický článek
Protein identification from electron cryomicroscopy maps by automated model building and side‐chain matching.
Autor: Terwilliger, Thomas C.1,2 (AUTHOR) tterwilliger@newmexicoconsortium.org, Sobolev, Oleg V.3 (AUTHOR), Afonine, Pavel V.3 (AUTHOR), Adams, Paul D.3,4 (AUTHOR), Ho, Chi-Min5,6,7,8 (AUTHOR), Li, Xiaorun7,9 (AUTHOR), Zhou, Z. Hong5,6,7 (AUTHOR)
Publikováno v: Acta Crystallographica: Section D, Structural Biology. Apr2021, Vol. 77 Issue 4, p457-462. 6p.
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10
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