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Reliability and accuracy of single-molecule FRET studies for characterization of structural dynamics and distances in proteins.
Ganesh Agam, Christian Gebhardt, Milana Popara, Rebecca Mächtel, Julian Folz, Benjamin Ambrose, Neharika Chamachi, Sang Yoon Chung, Timothy D Craggs, Marijn de Boer, Dina Grohmann, Taekjip Ha, Andreas Hartmann, Jelle Hendrix, Verena Hirschfeld, Christian G Hübner, Thorsten Hugel, Dominik Kammerer, Hyun-Seo Kang, Achillefs N Kapanidis, Georg Krainer, Kevin Kramm, Edward A Lemke, Eitan Lerner, Emmanuel Margeat, Kirsten Martens, Jens Michaelis, Jaba Mitra, Gabriel G Moya Muñoz, Robert B Quast, Nicole C Robb, Michael Sattler, Michael Schlierf, Jonathan Schneider, Tim Schröder, Anna Sefer, Piau Siong Tan, Johann Thurn, Philip Tinnefeld, John van Noort, Shimon Weiss, Nicolas Wendler, Niels Zijlstra, Anders Barth, Claus A M Seidel, Don C Lamb, Thorben Cordes
Apr 17, 2023
Single-molecule Förster-resonance energy transfer (smFRET) experiments allow the study of biomolecular structure and dynamics in vitro and in vivo. We performed an international blind study involving 19 laboratories to assess...
Proteins Fluorescence Resonance Energy Transfer Reproducibility of Results Molecular Conformation Laboratories
Published by: Nature methods
Likelihood-based docking of models into cryo-EM maps.
Optimized docking of models into cryo-EM maps requires exploiting an understanding of the signal expected in the data to minimize the calculation time while maintaining sufficient signal. The likelihood-based rotation function...
Multidimensional Protein Solubility Optimization with an Ultrahigh-Throughput Microfluidic Platform.