title: Volta phase plate cryo-EM of the small protein complex Prx3.
abstract: Cryo-EM of large, macromolecular assemblies has seen a significant increase in the numbers of high-resolution structures since the arrival of direct electron detectors. However, sub-nanometre resolution cryo-EM structures are rare compared with crystal structure depositions, particularly for relatively small particles (<400 kDa). Here we demonstrate the benefits of Volta phase plates for single-particle analysis by time-efficient cryo-EM structure determination of 257 kDa human peroxiredoxin-3 dodecamers at 4.4 Å resolution. The Volta phase plate improves the applicability of cryo-EM for small molecules and accelerates structure determination.
authors.affiliation: Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.
authors.forename: Maryam
authors.initials: M
authors.lastname: Khoshouei
authors.affiliation: School of Biological Sciences, University of Auckland, Auckland 1042, New Zealand.|Department of Biochemistry and Molecular Biology, Monash University, Victoria, 3800 Melbourne, Australia.
authors.forename: Mazdak
authors.initials: M
authors.lastname: Radjainia
authors.affiliation: Lincoln Agritech Limited, Lincoln 7640, New Zealand.
authors.forename: Amy J
authors.initials: AJ
authors.lastname: Phillips
authors.affiliation: School of Biological Sciences, University of Auckland, Auckland 1042, New Zealand.|MacDiarmid Institute for Advanced Materials and Nanotechnology, Victoria University, Wellington 6140, New Zealand.|School of Chemical Sciences, University of Auckland, 23 Symonds Street, Auckland 1010, New Zealand.
authors.forename: Juliet A
authors.initials: JA
authors.lastname: Gerrard
authors.affiliation: School of Biological Sciences, University of Auckland, Auckland 1042, New Zealand.
authors.forename: Alok K
authors.initials: AK
authors.lastname: Mitra
authors.affiliation: Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.
authors.forename: Jürgen M
authors.initials: JM
authors.lastname: Plitzko
authors.affiliation: Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Baumeister
authors.affiliation: Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.
authors.forename: Radostin
authors.initials: R
authors.lastname: Danev
mesh_terms: D020285:Cryoelectron Microscopy / Q000295:instrumentation / Q000379:methods*; D006801:Humans; D046912:Multiprotein Complexes / Q000737:chemistry*; D061105:Peroxiredoxin III / Q000737:chemistry*
chemical_list: D046912:Multiprotein Complexes; C516115:PRDX3 protein, human; D061105:Peroxiredoxin III
references.citation: Ultramicroscopy. 2012 May;116:62-72
references.pmid: 22537744
references.citation: Biomacromolecules. 2014 May 12;15(5):1871-81
references.pmid: 24749984
references.citation: Proc Natl Acad Sci U S A. 2014 Nov 4;111(44):15635-40
references.pmid: 25331897
references.citation: J Electron Microsc (Tokyo). 2011;60 Suppl 1:S43-62
references.pmid: 21844600
references.citation: Cell. 2015 Jul 16;162(2):314-27
references.pmid: 26144317
references.citation: J Struct Biol. 2015 Mar;189(3):163-76
references.pmid: 25681631
references.citation: Nat Methods. 2013 Jun;10(6):584-90
references.pmid: 23644547
references.citation: J Struct Biol. 2005 Oct;152(1):36-51
references.pmid: 16182563
references.citation: Science. 2015 Jun 5;348(6239):1147-51
references.pmid: 25953817
references.citation: Q Rev Biophys. 1995 May;28(2):171-93
references.pmid: 7568675
references.citation: Cell. 2015 Apr 23;161(3):438-49
references.pmid: 25910204
references.citation: Structure. 2005 Nov;13(11):1661-4
references.pmid: 16271889
references.citation: Science. 2014 Mar 28;343(6178):1443-4
references.pmid: 24675944
references.citation: Structure. 2010 Aug 11;18(8):903-12
references.pmid: 20696391
references.citation: Structure. 2000 Jun 15;8(6):605-15
references.pmid: 10873855
references.citation: J Struct Biol. 2007 Jan;157(1):281-7
references.pmid: 16963278
references.citation: J Struct Biol. 2007 Jan;157(1):38-46
references.pmid: 16859925
references.citation: Nature. 2015 Sep 10;525(7568):212-7
references.pmid: 26280335
references.citation: Nature. 2013 Dec 5;504(7478):107-12
references.pmid: 24305160
references.citation: Structure. 2010 Jan 13;18(1):17-27
references.pmid: 20152149
references.citation: Structure. 2015 May 5;23(5):912-20
references.pmid: 25914057
references.citation: J Mol Biol. 2012 Jan 13;415(2):406-18
references.pmid: 22100448
references.citation: Science. 2015 Jan 23;347(6220):439-42
references.pmid: 25613890
references.citation: Free Radic Biol Med. 2008 Sep 1;45(5):549-61
references.pmid: 18544350