Hostname: page-component-7479d7b7d-fwgfc Total loading time: 0 Render date: 2024-07-12T01:35:12.759Z Has data issue: false hasContentIssue false

Cryo-EM Analysis and de Novo Modeling of E. coli dihydrolipoamide Succinyltransferase Catalytic Domain Structure

Published online by Cambridge University Press:  30 July 2020

Vasily Mikirtumov
Affiliation:
Moscow Lomonosov University, moscow, Moskva, Russia
Evgeny Pichkur
Affiliation:
Kurchatov Institute, Moscow, Moskva, Russia
Olga Tikhonova
Affiliation:
Orekhovich Research Institute of Biomedical Chemistry RAS, Moscow, Moskva, Russia
Lidia Kurochkina
Affiliation:
Belozersky Research Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, Moscow, Moskva, Russia
Olga Sokolova
Affiliation:
Lomonosov Moscow State University, Faculty of Biology, Moscow, Moskva, Russia

Abstract

Image of the first page of this content. For PDF version, please use the ‘Save PDF’ preceeding this image.'
Type
3D Structures: From Macromolecular Assemblies to Whole Cells (3DEM FIG)
Copyright
Copyright © Microscopy Society of America 2020

References

Scheres, S.H.W. Journal of structural biology 180.3 (2012): 519530.10.1016/j.jsb.2012.09.006CrossRefGoogle Scholar
Punjani, A., et al. Nature methods 14.3 (2017): 290.10.1038/nmeth.4169CrossRefGoogle Scholar
Emsley, P., et al. “Features and development of Coot.” Acta Crystallographica Section D: Biological Crystallography 66.4 (2010): 486501.10.1107/S0907444910007493CrossRefGoogle ScholarPubMed
Knapp, J.E., et al. Journal of molecular biology 280.4 (1998): 655668.10.1006/jmbi.1998.1924CrossRefGoogle Scholar
Andi, B., et al. Acta Crystallographica Section F: Structural Biology Communications 75.9 (2019): 616624.Google Scholar
Cryo-EM sample preparation was performed using the “3D-EMС” instrument cluster of Moscow State University (supported by the Ministry of science and higher education of Russian Federation, unique identifier RFMEFI61919X0014).Google Scholar