Serious issues with cryo-EM structures of human prothrombinase by James A. Huntington, Alexandre Faille, Fatma Isik Ustok

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Cryo-EM structure of an activated GPR4–Gs signaling complex by Yitong Ma, Yijie Wang, Mengyuan Tang, Yuan Weng, Ying Chen, Yueming Xu, Shuxiao An, Yiran Wu, Suwen Zhao, Huanhuan Xu, Dali Li, Mingyao Liu, Weiqiang Lu, Heng Ru, Gaojie Song

“…Here we report cryo-electron microscopy (cryo-EM) structures of active zebrafish GPR4 at both pH 6.5 and 8.5, each highlighting a distribution of histidine and acidic residues at the extracellular region. …”
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Scaffold-enabled high-resolution cryo-EM structure determination of RNA by Daniel B. Haack, Boris Rudolfs, Shouhong Jin, Alexandra Khitun, Kevin M. Weeks, Navtej Toor

“…Abstract Cryo-EM structure determination of protein-free RNAs has remained difficult with most attempts yielding low to moderate resolution and lacking nucleotide-level detail. …”
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Parallelizing the cryo‐EM structure determination in THUNDER using GPU cluster by Zhao Wang, Huabin Ruan, Guangwen Yang, Xueming Li

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Cryo-EM structure and evolutionary history of the conjugation surface exclusion protein TraT by Chloe Seddon, Sophia David, Joshua L. C. Wong, Naito Ishimoto, Shan He, Jonathan Bradshaw, Wen Wen Low, Gad Frankel, Konstantinos Beis

“…Here, we show that TraT from the pKpQIL and F plasmids (TraTpKpQIL and TraTF) exhibits plasmid surface exclusion specificity. The cryo-EM structures of TraTpKpQIL and TraTF reveal that they oligomerise into decameric champagne bottle cork-like structures, which are anchored to the outer membrane via a diacylglycerol and palmitic acid modified α-helical barrel domain. …”
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Protein identification using Cryo-EM and artificial intelligence guides improved sample purification by Kenneth D. Carr, Dane Evan D. Zambrano, Connor Weidle, Alex Goodson, Helen E. Eisenach, Harley Pyles, Alexis Courbet, Neil P. King, Andrew J. Borst

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The dynamic duo: cryo-EM teams up with machine learning to visualize biomolecules in motion by Beatrice Bowlby

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Non-uniform Fourier transform based image classification in single-particle Cryo-EM by ZiJian Bai, Jian Huang

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Structure of an ex vivoDrosophila TOM complex determined by single-particle cryoEM by Agalya Periasamy, Pamela Ornelas, Thomas Bausewein, Naomi Mitchell, Jiamin Zhao, Leonie M. Quinn, Werner Kuehlbrandt, Jacqueline M. Gulbis

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AI-based quality assessment methods for protein structure models from cryo-EM by Han Zhu, Genki Terashi, Farhanaz Farheen, Tsukasa Nakamura, Daisuke Kihara

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Protocol for estimating the contrast transfer function and absolute tilt angle offset for cryo-electron tomography using CTFMeasure by Ranhao Zhang, Yuan Shen, Xueming Li

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High-resolution Cryo-EM Structure Determination of a-Synuclein—A Prototypical Amyloid Fibril by Juan Sanchez, Joshua Pierson, Collin Borcik, Chad Rienstra, Elizabeth Wright

“…We provide a detailed step-by-step protocol for high-resolution cryo-EM structure determination of a-syn fibrils using RELION and a series of specialized helical reconstruction tools that can be run within RELION. …”
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Cryo-EM structure and oligomerization of the human planar cell polarity core protein Vangl1 by Fan Zhang, Shaobai Li, Hao Wu, Shanshuang Chen

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Structural studies of the IFNλ4 receptor complex using cryoEM enabled by protein engineering by William S. Grubbe, Bixia Zhang, Aileen Kauffman, Fabian Byléhn, Kasia Padoł, Hae-Gwang Jung, Seung Bum Park, Jessica M. Priest, Engin Özkan, Juan J. de Pablo, T. Jake Liang, Minglei Zhao, Juan L. Mendoza

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Cryo-EM structure of the calcium-sensing receptor complexed with the kokumi substance γ-glutamyl-valyl-glycine by Hiroki Yamaguchi, Seiji Kitajima, Hiroshi Suzuki, Shota Suzuki, Kouki Nishikawa, Akiko Kamegawa, Yoshinori Fujiyoshi, Kazutoshi Takahashi, Uno Tagami, Yutaka Maruyama, Motonaka Kuroda, Masayuki Sugiki

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Cryo-EM structure of Sudan ebolavirus glycoprotein complexed with its human endosomal receptor NPC1 by Fan Bu, Gang Ye, Hailey Turner-Hubbard, Morgan Herbst, Bin Liu, Fang Li

“…The findings reveal that the SUDV glycoprotein binds significantly more strongly to hNPC1 than the EBOV glycoprotein. Using cryo-EM, we determined the structure of the SUDV glycoprotein/hNPC1 complex, identifying four key residues in the SUDV glycoprotein that differ from those in the EBOV glycoprotein and influence hNPC1 binding: Ile79, Ala141, and Pro148 enhance binding, while Gln142 reduces it. …”
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CryoEM structure and small-angle X-ray scattering analyses of porcine retinol-binding protein 3 by Vineeta Kaushik, Luca Gessa, Nelam Kumar, Matyáš Pinkas, Mariusz Czarnocki-Cieciura, Krzysztof Palczewski, Jiří Nováček, Humberto Fernandes

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The Cryo-EM structure of human CD163 bound to haptoglobin-hemoglobin reveals molecular mechanisms of hemoglobin scavenging by Anders Etzerodt, Jakob Hauge Mikkelsen, Morten Torvund-Jensen, Dorle Hennig, Thomas Boesen, Jonas Heilskov Graversen, Søren Kragh Moestrup, Justin M. Kollman, Christian Brix Folsted Andersen

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A fiducial-assisted strategy compatible with resolving small MFS transporter structures in multiple conformations using cryo-EM by Pujun Xie, Yan Li, Gaëlle Lamon, Huihui Kuang, Da-Neng Wang, Nathaniel J. Traaseth

“…Abstract Advancements in cryo-EM have stimulated a revolution in structural biology. …”
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Structural insights into HIV-2 CA lattice formation and FG-pocket binding revealed by single-particle cryo-EM by Matthew Cook, Christian Freniere, Chunxiang Wu, Faith Lozano, Yong Xiong

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