Electron microscopy of biotinylated protein complexes bound to streptavidin monolayer crystals

Journal of Structural Biology
Bong-Gyoon HanR M Glaeser

Abstract

Chemical biotinylation of protein complexes followed by binding to two-dimensional (monolayer) crystals of streptavidin is shown to be an effective way to prepare cryo-EM specimens from samples at low protein concentration. Three different multiprotein complexes are used to demonstrate the generality of this method. In addition, native thermosomes, purified from Sulfolobus solfataricus P2, are used to demonstrate that a uniform distribution of Euler angles is produced, even though this particle is known to adopt a preferred orientation when other methods of cryo-EM specimen preparation are used.

References

Apr 22, 2004·Journal of Structural Biology·Corinne CrucifixPatrick Schultz
Jan 5, 2005·Journal of Structural Biology·Dieter TypkeRobert M Glaeser
Mar 19, 2008·Proceedings of the National Academy of Sciences of the United States of America·Deborah F KellyThomas Walz
Jul 29, 2008·Journal of Molecular Biology·Deborah F KellyThomas Walz
Oct 7, 2009·Proceedings of the National Academy of Sciences of the United States of America·Bong-Gyoon HanRobert M Glaeser

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Citations

Jan 18, 2016·Current Opinion in Structural Biology·Christopher J Russo, Lori A Passmore
Jun 21, 2016·Journal of Structural Biology·Bong-Gyoon HanRobert M Glaeser
Sep 4, 2018·Microscopy and Microanalysis : the Official Journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada·Rebecca S DillardElizabeth R Wright
Aug 7, 2017·Biophysical Reports·Robert M Glaeser, Bong-Gyoon Han
Sep 12, 2020·Proceedings of the National Academy of Sciences of the United States of America·Feng WangDavid A Agard
Mar 6, 2017·Journal of Structural Biology·Bong-Gyoon HanRobert M Glaeser
Mar 5, 2020·Journal of Chemical Information and Modeling·Caitlyn L McCaffertyDavid W Taylor

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