"Our aim is to provide a forum for rapid publication of important results in the cryoEM field. We seek to publish methodological advances as well as new biologically relevant findings that emerge from the use of cryoEM and related techniques."

Professor Sriram Subramaniam

main editor for cryoEM

S. SubramaniamFaculty of Medicine, University of British Columbia, Vancouver, BC V6T 1Z3, Canada (e-mail: sriram.subramaniam@ubc.ca)

co-editors

E. BullittDepartment of Physiology & Biophysics, Boston University School of Medicine, 700 Albany St, Boston MA 02118-2526, USA (e-mail: bullitt@bu.edu)
W. KühlbrandtDepartment of Structural Biology, Max Planck Institute of Biophysics, Max von Laue-Str. 3, 60438 Frankfurt am Main, Germany (e-mail: werner.kuehlbrandt@biophys.mpg.de)
S. RaunserDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Otto-Hahn-Str. 11, 44227 Dortmund, Germany (e-mail: stefan.raunser@mpi-dortmund.mpg.de)
F. SunInstitute of Biophysics, Chinese Academy of Sciences, School of Life Science, University of Chinese Academy of Sciences, Datun Road 15, Chaoyang District, Beijing 100101, China (e-mail: feisun@ibp.ac.cn)

articles in this subject area

Community recommendations on cryoEM data archiving and validation. G. J. Kleywegt, P. D. Adams, S. J. Butcher, C. L. Lawson, A. Rohou, P. B. Rosenthal, S. Subramaniam, M. Topf, S. Abbott, P. R. Baldwin, J. M. Berrisford, G. Bricogne, P. Choudhary, T. I. Croll, R. Danev, S. J. Ganesan, T. Grant, A. Gutmanas, R. Henderson, J. B. Heymann, J. T. Huiskonen, A. Istrate, T. Kato, G. C. Lander, S.-M. Lok, S. J. Ludtke, G. N. Murshudov, R. Pye, G. D. Pintilie, J. S. Richardson, C. Sachse, O. Salih, S. H. W. Scheres, G. F. Schroeder, C. O. S. Sorzano, S. M. Stagg, Z. Wang, R. Warshamanage, J. D. Westbrook, M. D. Winn, J. Y. Young, S. K. Burley, J. C. Hoch, G. Kurisu, K. Morris, A. Patwardhan & S. Velankar (2024). IUCrJ 11, 140-151. 
C-SPAM: an open-source time-resolved specimen vitrification device with light-activated molecules. A. Montaño Romero, C. Bonin & E. C. Twomey (2024). IUCrJ 11, 16-22. 
MRC2020: improvements to Ximdisp and the MRC image-processing programs. J. M. Short, C. M. Palmer, T. Burnley, M. D. Winn, Q. Zhang, B. V. Venkataram Prasad, S. Chen, R. A. Crowther, P. N. T. Unwin & R. Henderson (2023). IUCrJ 10, 579-583. 
`Cryo-EM': electron cryomicroscopy, cryo electron microscopy or something else?. R. Henderson & S. Hasnain (2023). IUCrJ 10, 519-520. 
Dynamical scattering in ice-embedded proteins in conventional and scanning transmission electron microscopy. M. L. Leidl, C. Sachse & K. Müller-Caspary (2023). IUCrJ 10, 475-486. 
Learning to automate cryo-electron microscopy data collection with Ptolemy. P. T. Kim, A. J. Noble, A. Cheng & T. Bepler (2023). IUCrJ 10, 90-102. 
Fully automated multi-grid cryoEM screening using Smart Leginon. A. Cheng, P. T. Kim, H. Kuang, J. H. Mendez, E. Y. D. Chua, K. Maruthi, H. Wei, A. Sawh, M. F. Aragon, V. Serbynovskyi, K. Neselu, E. T. Eng, C. S. Potter, B. Carragher, T. Bepler & A. J. Noble (2023). IUCrJ 10, 77-89. 
Analysis of the conformational heterogeneity of the Rieske iron–sulfur protein in complex III2 by cryo-EM. J.-P. Wieferig & W. Kühlbrandt (2023). IUCrJ 10, 27-37. 
Towards automating single-particle cryo-EM data acquisition. C. Dienemann (2023). IUCrJ 10, 4-5. 
Structural heterogeneity of the Rieske iron–sulfur protein in a yeast complex III2. K. R. Vinothkumar (2023). IUCrJ 10, 1-3. 
Analytic modeling of inhomogeneous-resolution maps in cryo-electron microscopy and crystallography. A. Urzhumtsev & V. Y. Lunin (2022). IUCrJ 9, 728-734. 
Making ripples in the comparison of calculated and experimental maps for real-space refinement and assessment by analytic modelling of local resolution. I. Usón (2022). IUCrJ 9, 718-719. 
Cryo-EM at ACA 2022. S. Subramaniam, A. Kotecha & J. H. Davis (2022). IUCrJ 9, 713-714. 
Higher resolution in cryo-EM by the combination of macromolecular prior knowledge and image-processing tools. E. Ramírez-Aportela, J. M. Carazo & C. O. S. Sorzano (2022). IUCrJ 9, 632-638. 
High-speed high-resolution data collection on a 200 keV cryo-TEM. J. V. Peck, J. F. Fay & J. D. Strauss (2022). IUCrJ 9, 243-252. 
Comparison of side-chain dispersion in protein structures determined by cryo-EM and X-ray crystallography. A. Ravikumar, M. N. Gopnarayan, S. Subramaniam & N. Srinivasan (2022). IUCrJ 9, 98-103. 
findMySequence: a neural-network-based approach for identification of unknown proteins in X-ray crystallography and cryo-EM. G. Chojnowski, A. J. Simpkin, D. A. Leonardo, W. Seifert-Davila, D. E. Vivas-Ruiz, R. M. Keegan & D. J. Rigden (2022). IUCrJ 9, 86-97. 
TRPV1 and Piezo: the 2021 Nobel Prize in Physiology or Medicine. Y. Cheng (2022). IUCrJ 9, 4-5. 
Approximating deformation fields for the analysis of continuous heterogeneity of biological macromolecules by 3D Zernike polynomials. D. Herreros, R. R. Lederman, J. Krieger, A. Jiménez-Moreno, M. Martínez, D. Myška, D. Strelak, J. Filipovic, I. Bahar, J. M. Carazo & C. O. S. Sanchez (2021). IUCrJ 8, 992-1005. 
Cryo-TEM simulations of amorphous radiation-sensitive samples using multislice wave propagation. B. Himes & N. Grigorieff (2021). IUCrJ 8, 943-953. 
High-resolution single-particle cryo-EM of samples vitrified in boiling nitro­gen. T. Engstrom, J. A. Clinger, K. A. Spoth, O. B. Clarke, D. S. Closs, R. Jayne, B. A. Apker & R. E. Thorne (2021). IUCrJ 8, 867-877. 
Cryo-EM structure of a thermostable bacterial nanocompartment. T. Wiryaman & N. Toor (2021). IUCrJ 8, 342-350. 
Cryo-EM structure of a thermophilic encapsulin offers clues to its functions. J. R. Castón (2021). IUCrJ 8, 333-334. 
Devitrification reduces beam-induced movement in cryo-EM. J.-P. Wieferig, D. J. Mills & W. Kühlbrandt (2021). IUCrJ 8, 186-194. 
Exploiting prior knowledge about biological macromolecules in cryo-EM structure determination. D. Kimanius, G. Zickert, T. Nakane, J. Adler, S. Lunz, C.-B. Schönlieb, O. Öktem & S. H. W. Scheres (2021). IUCrJ 8, 60-75. 
High-resolution cryo-EM using beam-image shift at 200 keV. J. N. Cash, S. Kearns, Y. Li & M. A. Cianfrocco (2020). IUCrJ 7, 1179-1187. 
Enhancing the signal-to-noise ratio and generating contrast for cryo-EM images with convolutional neural networks. E. Palovcak, D. Asarnow, M. G. Campbell, Z. Yu & Y. Cheng (2020). IUCrJ 7, 1142-1150. 
Continuous flexibility analysis of SARS-CoV-2 spike prefusion structures. R. Melero, C. O. S. Sorzano, B. Foster, J.-L. Vilas, M. Martínez, R. Marabini, E. Ramírez-Aportela, R. Sanchez-Garcia, D. Herreros, L. del Caño, P. Losana, Y. C. Fonseca-Reyna, P. Conesa, D. Wrapp, P. Chacon, J. S. McLellan, H. D. Tagare & J.-M. Carazo (2020). IUCrJ 7, 1059-1069. 
Reliable cryo-EM resolution estimation with modified Fourier shell correlation. P. A. Penczek (2020). IUCrJ 7, 995-1008. 
Deep learning enables the atomic structure determination of the Fanconi Anemia core complex from cryoEM. D. P. Farrell, I. Anishchenko, S. Shakeel, A. Lauko, L. A. Passmore, D. Baker & F. DiMaio (2020). IUCrJ 7, 881-892. 
Electron-event representation data enable efficient cryoEM file storage with full preservation of spatial and temporal resolution. H. Guo, E. Franken, Y. Deng, S. Benlekbir, G. Singla Lezcano, B. Janssen, L. Yu, Z. A. Ripstein, Y. Z. Tan & J. L. Rubinstein (2020). IUCrJ 7, 860-869. 
Protein–lipid architecture of a cholinergic postsynaptic membrane. N. Unwin (2020). IUCrJ 7, 852-859. 
Electrons receive individual treatment with electron-event representation. R. Danev (2020). IUCrJ 7, 780-781. 
A self-supervised workflow for particle picking in cryo-EM. D. M. McSweeney, S. M. McSweeney & Q. Liu (2020). IUCrJ 7, 719-727. 
Assessing the JEOL CRYO ARM 300 for high-throughput automated single-particle cryo-EM in a multiuser environment. M. Fislage, A. V. Shkumatov, A. Stroobants & R. G. Efremov (2020). IUCrJ 7, 707-718. 
1.8 Å resolution structure of β-galactosidase with a 200 kV CRYO ARM electron microscope. A. Merk, T. Fukumura, X. Zhu, J. E. Darling, R. Grisshammer, J. Ognjenovic & S. Subramaniam (2020). IUCrJ 7, 639-643. 
COVID-19 and cryo-EM. S. Subramaniam (2020). IUCrJ 7, 575-576. 
Fast and accurate defocus modulation for improved tunability of cryo-EM experiments. R. Danev, H. Iijima, M. Matsuzaki & S. Motoki (2020). IUCrJ 7, 566-574. 
Atomic structures determined from digitally defined nanocrystalline regions. M. Gallagher-Jones, K. C. Bustillo, C. Ophus, L. S. Richards, J. Ciston, S. Lee, A. M. Minor & J. A. Rodriguez (2020). IUCrJ 7, 490-499. 
Plasmodium vivax and human hexokinases share similar active sites but display distinct quaternary architectures. S. S. Srivastava, J. E. Darling, J. Suryadi, J. C. Morris, M. E. Drew & S. Subramaniam (2020). IUCrJ 7, 453-461. 
High-resolution cryo-EM reconstructions in the presence of substantial aberrations. R. Bromberg, Y. Guo, D. Borek & Z. Otwinowski (2020). IUCrJ 7, 445-452. 
Hypothesis for a mechanism of beam-induced motion in cryo-electron microscopy. R. E. Thorne (2020). IUCrJ 7, 416-421. 
The active form of quinol-dependent nitric oxide reductase from Neisseria meningitidis is a dimer. M. A. M. Jamali, C. C. Gopalasingam, R. M. Johnson, T. Tosha, K. Muramoto, S. P. Muench, S. V. Antonyuk, Y. Shiro & S. S. Hasnain (2020). IUCrJ 7, 404-415. 
Estimation of high-order aberrations and anisotropic magnification from cryo-EM data sets in RELION-3.1. J. Zivanov, T. Nakane & S. H. W. Scheres (2020). IUCrJ 7, 253-267. 
The resolution revolution in cryoEM requires high-quality sample preparation: a rapid pipeline to a high-resolution map of yeast fatty acid synthase. M. Joppe, E. D'Imprima, N. Salustros, K. S. Paithankar, J. Vonck, M. Grininger & W. Kühlbrandt (2020). IUCrJ 7, 220-227. 
A comparative study of single-particle cryo-EM with liquid-nitrogen and liquid-helium cooling. O. Pfeil-Gardiner, D. J. Mills, J. Vonck & W. Kuehlbrandt (2019). IUCrJ 6, 1099-1105. 
CryoEM at 100 keV: a demonstration and prospects. K. Naydenova, G. McMullan, M. J. Peet, Y. Lee, P. C. Edwards, S. Chen, E. Leahy, S. Scotcher, R. Henderson & C. J. Russo (2019). IUCrJ 6, 1086-1098. 
DeepRes: a new deep-learning- and aspect-based local resolution method for electron-microscopy maps. E. Ramírez-Aportela, J. Mota, P. Conesa, J. M. Carazo & C. O. S. Sorzano (2019). IUCrJ 6, 1054-1063. 
A cryo-EM grid preparation device for time-resolved structural studies. D. Kontziampasis, D. P. Klebl, M. G. Iadanza, C. A. Scarff, F. Kopf, F. Sobott, D. C. F. Monteiro, M. Trebbin, S. P. Muench & H. D. White (2019). IUCrJ 6, 1024-1031. 
Throughput and resolution with a next-generation direct electron detector. J. H. Mendez, A. Mehrani, P. Randolph & S. Stagg (2019). IUCrJ 6, 1007-1013. 
A potential difference for single-particle cryo-EM. P. B. Rosenthal (2019). IUCrJ 6, 988-989. 
MicroED with the Falcon III direct electron detector. J. Hattne, M. W. Martynowycz, P. A. Penczek & T. Gonen (2019). IUCrJ 6, 921-926. 
Cryo-EM structure of the CFA/I pilus rod. W. Zheng, M. Andersson, N. Mortezaei, E. Bullitt & E. Egelman (2019). IUCrJ 6, 815-821. 
Cryo-EM structure of Neurospora crassa respiratory complex IV. T. Bausewein, S. Nussberger & W. Kühlbrandt (2019). IUCrJ 6, 773-780. 
Namdinator – automatic molecular dynamics flexible fitting of structural models into cryo-EM and crystallography experimental maps. R. T. Kidmose, J. Juhl, P. Nissen, T. Boesen, J. L. Karlsen & B. P. Pedersen (2019). IUCrJ 6, 526-531. 
Cryo-EM reveals the asymmetric assembly of squid hemocyanin. Y. Tanaka, S. Kato, M. Stabrin, S. Raunser, T. Matsui & C. Gatsogiannis (2019). IUCrJ 6, 426-437. 
Homochiral and racemic MicroED structures of a peptide repeat from the ice-nucleation protein InaZ. C. Zee, C. Glynn, M. Gallagher-Jones, J. Miao, C. G. Santiago, D. Cascio, T. Gonen, M. R. Sawaya & J. A. Rodriguez (2019). IUCrJ 6, 197-205. 
Nanobeam precession-assisted 3D electron diffraction reveals a new polymorph of hen egg-white lysozyme. A. Lanza, E. Margheritis, E. Mugnaioli, V. Cappello, G. Garau & M. Gemmi (2019). IUCrJ 6, 178-188. 
Thresholding of cryo-EM density maps by false discovery rate control. M. Beckers, A. J. Jakobi & C. Sachse (2019). IUCrJ 6, 18-33. 
A Bayesian approach to beam-induced motion correction in cryo-EM single-particle analysis. J. Zivanov, T. Nakane & S. H. W. Scheres (2019). IUCrJ 6, 5-17. 
Interpreting the cryo-EM map. P. B. Rosenthal (2019). IUCrJ 6, 3-4. 
The cryo-EM revolution: fueling the next phase. S. Subramaniam (2019). IUCrJ 6, 1-2. 
Deep Consensus, a deep learning-based approach for particle pruning in cryo-electron microscopy. R. Sanchez-Garcia, J. Segura, D. Maluenda, J. M. Carazo & C. O. S. Sorzano (2018). IUCrJ 5, 854-865. 
Using cryo-electron microscopy maps for X-ray structure determination. L. Zeng, W. Ding & Q. Hao (2018). IUCrJ 5, 382-389. 
Identification of ions in experimental electrostatic potential maps. J. Wang, Z. Liu, J. Frank & P. B. Moore (2018). IUCrJ 5, 375-381. 
Ionic scattering factors of atoms that compose biological molecules. K. Yonekura, R. Matsuoka, Y. Yamashita, T. Yamane, M. Ikeguchi, A. Kidera & S. Maki-Yonekura (2018). IUCrJ 5, 348-353. 
X-ray and cryo-EM structures of inhibitor-bound cytochrome bc1 complexes for structure-based drug discovery. K. Amporndanai, R. M. Johnson, P. M. O'Neill, C. W. G. Fishwick, A. H. Jamson, S. Rawson, S. P. Muench, S. S. Hasnain & S. V. Antonyuk (2018). IUCrJ 5, 200-210. 
Cryo-EM reconstruction of the chlororibosome to 3.2 Å resolution within 24 h. B. O. Forsberg, S. Aibara, D. Kimanius, B. Paul, E. Lindahl & A. Amunts (2017). IUCrJ 4, 723-727. 
Single-particle cryo-EM using alignment by classification (ABC): the structure of Lumbricus terrestris haemoglobin. P. Afanasyev, C. Seer-Linnemayr, R. B. G. Ravelli, R. Matadeen, S. De Carlo, B. Alewijnse, R. V. Portugal, N. S. Pannu, M. Schatz & M. van Heel (2017). IUCrJ 4, 678-694. 
Segregation of lipids near acetylcholine-receptor channels imaged by cryo-EM. N. Unwin (2017). IUCrJ 4, 393-399. 
CryoEM at IUCrJ: a new era. S. Subramaniam, W. Kühlbrandt & R. Henderson (2016). IUCrJ 3, 3-7. 

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