Localized reconstruction in Scipion expedites the analysis of symmetry mismatches in cryo-EM data

作者: Vahid Abrishami , Serban L. Ilca , Josue Gomez-Blanco , Ilona Rissanen , José Miguel de la Rosa-Trevín

DOI: 10.1016/J.PBIOMOLBIO.2020.05.004

关键词:

摘要: Abstract Technological advances in transmission electron microscopes and detectors have turned cryogenic microscopy (cryo-EM) into an essential tool for structural biology. A commonly used cryo-EM data analysis method, single particle analysis, averages hundreds of thousands low-dose images individual macromolecular complexes to determine a density map the complex. The presence symmetry complex is beneficial since each projection image can be assigned multiple views However, processing that applies average out asymmetric features consequently methods are required resolve features. Scipion framework integrates functions from different packages as plugins. To extend its functionality handling mismatches, we present here plugin termed LocalRec implementing localized reconstruction method. When tested on adenovirus set, enables resolving symmetry-mismatched trimeric fibre bound five-fold vertices capsid. Furthermore, it improves structure determination icosahedral capsid by dealing with defocus gradient across particle. expected widely applicable range investigations flexible mismatched complexes.

参考文章(29)
David J. DeRosier, Correction of high-resolution data for curvature of the Ewald sphere. Ultramicroscopy. ,vol. 81, pp. 83- 98 ,(2000) , 10.1016/S0304-3991(99)00120-5
Sjors H.W. Scheres, A Bayesian View on Cryo-EM Structure Determination Journal of Molecular Biology. ,vol. 415, pp. 406- 418 ,(2012) , 10.1016/J.JMB.2011.11.010
Fei Guo, Zheng Liu, Frank Vago, Yue Ren, Weimin Wu, Elena T Wright, Philip Serwer, Wen Jiang, None, Visualization of uncorrelated, tandem symmetry mismatches in the internal genome packaging apparatus of bacteriophage T7 Proceedings of the National Academy of Sciences of the United States of America. ,vol. 110, pp. 6811- 6816 ,(2013) , 10.1073/PNAS.1215563110
V. S. Reddy, S. K. Natchiar, P. L. Stewart, G. R. Nemerow, Crystal Structure of Human Adenovirus at 3.5 Å Resolution Science. ,vol. 329, pp. 1071- 1075 ,(2010) , 10.1126/SCIENCE.1187292
J.M. de la Rosa-Trevín, J. Otón, R. Marabini, A. Zaldívar, J. Vargas, J.M. Carazo, C.O.S. Sorzano, Xmipp 3.0: an improved software suite for image processing in electron microscopy. Journal of Structural Biology. ,vol. 184, pp. 321- 328 ,(2013) , 10.1016/J.JSB.2013.09.015
Marc C Morais, Yizhi Tao, Norman H Olson, Shelley Grimes, Paul J Jardine, Dwight L Anderson, Timothy S Baker, Michael G Rossmann, None, Cryoelectron-Microscopy Image Reconstruction of Symmetry Mismatches in Bacteriophage φ29 Journal of Structural Biology. ,vol. 135, pp. 38- 46 ,(2001) , 10.1006/JSBI.2001.4379
Xiao-chen Bai, Eeson Rajendra, Guanghui Yang, Yigong Shi, Sjors HW Scheres, Sampling the conformational space of the catalytic subunit of human γ-secretase eLife. ,vol. 4, ,(2015) , 10.7554/ELIFE.11182
A. Miyazawa, Y. Fujiyoshi, M. Stowell, N. Unwin, Nicotinic acetylcholine receptor at 4.6 Å resolution: transverse tunnels in the channel 1 1Edited by J. Karn Journal of Molecular Biology. ,vol. 288, pp. 765- 786 ,(1999) , 10.1006/JMBI.1999.2721
Serban L. Ilca, Abhay Kotecha, Xiaoyu Sun, Minna M. Poranen, David I. Stuart, Juha T. Huiskonen, Localized reconstruction of subunits from electron cryomicroscopy images of macromolecular complexes Nature Communications. ,vol. 6, pp. 8843- 8843 ,(2015) , 10.1038/NCOMMS9843
J.M. de la Rosa-Trevín, A. Quintana, L. del Cano, A. Zaldívar, I. Foche, J. Gutiérrez, J. Gómez-Blanco, J. Burguet-Castell, J. Cuenca-Alba, V. Abrishami, J. Vargas, J. Otón, G. Sharov, J.L. Vilas, J. Navas, P. Conesa, M. Kazemi, R. Marabini, C.O.S. Sorzano, J.M. Carazo, Scipion: A software framework toward integration, reproducibility and validation in 3D electron microscopy. Journal of Structural Biology. ,vol. 195, pp. 93- 99 ,(2016) , 10.1016/J.JSB.2016.04.010