title: High-resolution structure determination by continuous-rotation data collection in MicroED.
abstract: MicroED uses very small three-dimensional protein crystals and electron diffraction for structure determination. We present an improved data collection protocol for MicroED called 'continuous rotation'. Microcrystals are continuously rotated during data collection, yielding more accurate data. The method enables data processing with the crystallographic software tool MOSFLM, which resulted in improved resolution for the model protein lysozyme. These improvements are paving the way for the broad implementation and application of MicroED in structural biology.
authors.affiliation: Janelia Research Campus, Howard Hughes Medical Institute, Ashburn VA, USA.
authors.forename: Brent L
authors.initials: BL
authors.lastname: Nannenga
authors.affiliation: Janelia Research Campus, Howard Hughes Medical Institute, Ashburn VA, USA.
authors.forename: Dan
authors.initials: D
authors.lastname: Shi
authors.affiliation: Medical Research Council Laboratory of Molecular Biology, Cambridge, UK.
authors.forename: Andrew G W
authors.initials: AGW
authors.lastname: Leslie
authors.affiliation: Janelia Research Campus, Howard Hughes Medical Institute, Ashburn VA, USA.
authors.forename: Tamir
authors.initials: T
authors.lastname: Gonen
mesh_terms: D000465:Algorithms; D030562:Databases, Protein; D004583:Electrons; D021621:Imaging, Three-Dimensional / Q000379:methods*; D016247:Information Storage and Retrieval / Q000379:methods*; D007834:Lasers; D018715:Microscopy, Video / Q000379:methods*; D011487:Protein Conformation; D011506:Proteins / Q000648:ultrastructure*; D012399:Rotation; D053838:Scattering, Small Angle; D014961:X-Ray Diffraction / Q000379:methods*
chemical_list: D011506:Proteins
references.citation: Methods Mol Biol. 2013;955:153-69
references.pmid: 23132060
references.citation: Acta Crystallogr D Biol Crystallogr. 2011 Apr;67(Pt 4):235-42
references.pmid: 21460441
references.citation: Biophys J. 2002 May;82(5):2784-97
references.pmid: 11964264
references.citation: Science. 2012 Jul 20;337(6092):362-4
references.pmid: 22653729
references.citation: Acta Crystallogr D Biol Crystallogr. 2001 Aug;57(Pt 8):1119-26
references.pmid: 11468395
references.citation: Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):213-21
references.pmid: 20124702
references.citation: Acta Crystallogr D Biol Crystallogr. 2011 Apr;67(Pt 4):271-81
references.pmid: 21460445
references.citation: Acta Crystallogr D Biol Crystallogr. 2013 Jul;69(Pt 7):1204-14
references.pmid: 23793146
references.citation: J Appl Crystallogr. 2007 Aug 1;40(Pt 4):658-674
references.pmid: 19461840
references.citation: Acta Crystallogr D Biol Crystallogr. 1999 Oct;55(Pt 10):1703-17
references.pmid: 10531520
references.citation: J Appl Crystallogr. 2014 May 29;47(Pt 3):1140-1145
references.pmid: 24904248
references.citation: Acta Crystallogr D Biol Crystallogr. 2011 Apr;67(Pt 4):282-92
references.pmid: 21460446
references.citation: J Mol Biol. 1996 Jun 14;259(3):393-421
references.pmid: 8676377
references.citation: Elife. 2013 Nov 19;2:e01345
references.pmid: 24252878
references.citation: Ultramicroscopy. 2007 Jun-Jul;107(6-7):523-33
references.pmid: 17291687
references.citation: Nature. 2011 Feb 3;470(7332):73-7
references.pmid: 21293373
references.citation: Nature. 2014 Jan 9;505(7482):244-7
references.pmid: 24270807