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Author
Alvarez, Roberto 1 Andreasson, Jakob 1 Aquila, Andrew 1 Assalauova, Dameli 1 Balaur, Eugeniu 1 Bobkov, Sergey 1 Contreras, Alice 1 DeMirci, Hasan 1 Gelisio, Luca 1 Hajdu, Janos 1 Hogue, Brenda G 1 Hunter, Mark S 1 Ilyin, Viacheslav A 1 Khubbutdinov, Ruslan 1 Kim, Young Yong 1 Kirian, Richard A 1 Kurta, Ruslan P 1 Li, Haoyuan 1 McFadden, Matthew 1 Nazari, Reza 1
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Workplace
Australian Research Council Centre of Excell... 1 Biodesign Institute Center for Applied Struc... 1 Biodesign Institute Center for Immunotherapy... 1 Center for Free Electron Laser Science DESY ... 1 Department of Molecular Biology and Genetics... 1 Department of Physics Arizona State Universi... 1 Deutsches Elektronen Synchrotron DESY Notkes... 1 European XFEL Holzkoppel 4 Schenefeld D 2286... 1 Institute of Physics ELI Beamlines Academy o... 1 Laboratory of Molecular Biophysics Departmen... 1 Max Planck Institute for the Structure and D... 1 Moscow Institute of Physics and Technology M... 1 National Research Center 'Kurchatov Institut... 1 National Research Nuclear University MEPhI K... 1 Physics Department Stanford University 450 J... 1 SLAC National Accelerator Laboratory 2575 Sa... 1 School for Engineering of Matter Transport a... 1 School of Life Sciences Arizona State Univer... 1 School of Mathematics and Statistical Scienc... 1 Stanford PULSE Institute SLAC National Accel... 1
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Most cited article - PubMed ID 31513011
Electron cryo-microscopy of bacteriophage PR772 reveals the elusive vertex complex and the capsid architecture
PubMed
33209321
PubMed Central
PMC7642788
DOI
10.1107/s2052252520012798
PII: S2052252520012798
Knihovny.cz E-resources
An improved analysis for single-particle imaging (SPI) experiments, using the limited data, is presented here. Results are based on a study of bacteriophage PR772 performed at the Atomic, Molecular and Optical Science instrument at the Linac Coherent Light Source as part of the SPI initiative. Existing methods were modified to cope with the shortcomings of the experimental data: inaccessibility of information from half of the detector and a small fraction of single hits. The general SPI analysis workflow was upgraded with the expectation-maximization based classification of diffraction patterns and mode decomposition on the final virus-structure determination step. The presented processing pipeline allowed us to determine the 3D structure of bacteriophage PR772 without symmetry constraints with a spatial resolution of 6.9 nm. The obtained resolution was limited by the scattering intensity during the experiment and the relatively small number of single hits.
- Keywords
- XFELs, bacteriophage PR772, single-particle imaging, three-dimensional virus reconstruction,
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