{"id":535,"date":"2018-11-01T14:03:18","date_gmt":"2018-11-01T14:03:18","guid":{"rendered":"https:\/\/www.purdue.edu\/cryoem2018\/?page_id=535"},"modified":"2018-11-07T13:38:45","modified_gmt":"2018-11-07T13:38:45","slug":"posters","status":"publish","type":"page","link":"https:\/\/www.purdue.edu\/cryoem2018\/posters\/","title":{"rendered":"Posters"},"content":{"rendered":"<p style=\"text-align: center\">Posters will be displayed on Wednesday, November 7th, 2018 from 4:00pm\u00a0\u2014 5:00pm. If you are presenting, we ask that you\u00a0setup from anytime before 4:00pm on\u00a0Wednesday. You may leave the posters setup until the end of the day.<\/p>\n<hr \/>\n<p>1 |\u00a0<b>Nestor Zaluzec<\/b> Soft Matter and Biosystems \u00a0Microanalysis by Analytical Electron Microscopy<\/p>\n<p>2 |\u00a0\u00a0<b>Ziao Fu<\/b> The Structural Basis for Release Factor Activation during Translation Termination<\/p>\n<p>3 |\u00a0<b>Austin Dixon<\/b> Generating Properly Folded Neurotensin Receptor-1 Through Cell-Free Protein Synthesis<\/p>\n<p>4 |\u00a0\u00a0<b>Edoardo Dimprima<\/b> The Deadly Touch: Protein Denaturation at the Air-Water Interface and How to Prevent It<\/p>\n<p>5 |\u00a0<b>Ellen Zhong<\/b> Testing the Limits of Modern Heterogeneous Reconstruction Algorithms: the Autophagy Initiation Complex<\/p>\n<p>6 |\u00a0<b>Herve Celia<\/b> Structural Investigation of the Ton Membrane Protein Complex, a Bacterial Molecular Motor<\/p>\n<p>7 |\u00a0<b>Audray Harris<\/b> Probing the Organization and Conformation of Influenza Virus Hemagglutinin by Cryo-Electron Microscopy with Insights for Universal Influenza Vaccine Development<\/p>\n<p>8 |\u00a0<b>Qianglin Fang<\/b> First Near-Atomic Structure of a Giant Virus<\/p>\n<p>9 |\u00a0<b>Elisabeth Garland-Kuntz<\/b> Structural Insights into Phospholipase-C Activity: Direct Observation of Conformational Dynamics<\/p>\n<p>10 |\u00a0<b>S. Saif Hasan<\/b> Structural Insights into the Entry and Antibody Neurtalization of Eastern Equine Encephalitis Virus<\/p>\n<p>11 |\u00a0<b>Thomas Klose<\/b> Structural Studies of Tupanvirus<\/p>\n<p>12 |\u00a0<b>Madhumati Sevvana<\/b> Cryo-EM Structures of the Mature Zika Virus<br \/>\nand its Complex with a Potent Virus-Specific Antibody<\/p>\n<p>13 |<b>\u00a0Chen Sun<\/b> Sub-3 \u00c5 Apoferritin Structures Determined With Single Position Of Volta Phase Plate and the Full Range of Phase Shift<\/p>\n<p>14 |\u00a0<b>Matthew Therkelsen<\/b> Flaviviruses have Imperfect Icosahedral Symmetry<\/p>\n<p>15 |\u00a0<b>Frank Vago<\/b> The 2.6 \u00c5 Cryo-EM Structure of GII.4 Norovirus VA387 in Complex with its Cellular Attachment Factor<\/p>\n<p>16 |\u00a0\u00a0<b>Ravi Yadav<\/b>\u00a0 Structural Insight into NmLbpB\u2019s Interaction with Human Lactoferrin<\/p>\n<p>17 |\u00a0<b>Genki Terashi<\/b> De Novo Main-Chain Modeling for EM Maps using MAINMAST<\/p>\n<p>18 |\u00a0<b>Philip Baldwin<\/b> A Quality Assessment of the Sampling of Projection Views in Cryo-EM based on the Estimate of Effect on (Global) SSNR<\/p>\n<p>19 |\u00a0<b>Ignacio Mir Sanchis<\/b> Cryo-EM Approach to Study Staphylococcal<br \/>\nMobile Genetic Elements&#8217; Replication: Helicase Loading and Translocation<\/p>\n<p>20 |\u00a0\u00a0<b>Wei-Jen<\/b> <b>Tang<\/b> Ensemble Cryo-EM Elucidates the Mechanism of Insulin Capture and Degradation by Human Insulin Degrading Enzyme<\/p>\n<p>21 |\u00a0<b>Fuxing Zeng<\/b> Translation Termination on mRNAs Lacking a Stop Codon<\/p>\n<p>22 |\u00a0<b>Pierce O&#8217;Neil<\/b> Structure of Tetanus Neurotoxin and Nanodisc Complexes<\/p>\n<p>23 |<b>\u00a0Kelly Manthei <\/b>Examination of the LCAT-HDL Complex<\/p>\n<p>24 | \u00a0<b>Min Su<\/b> goCTF: Geometrically Optimized CTF Determination for Single-Particle Cryo-EM<\/p>\n<p>25 |<b>\u00a0Agnieszka Ruszkowska<\/b> Structural Insights into the RNA<br \/>\nMethyltransferase Domain of METTL16<\/p>\n<p>26 |\u00a0<b>Yan Zhang<\/b> CCT Conformational Space Elucidated by Elastic Network Model Analysis of Cryo-EM Data<\/p>\n<p>27 |\u00a0<b>Gavin Rice<\/b> Structural Characterization of Venom Peptide \u2013 Ion Channel Complexes: How the Resolution Revolution Can Improve Drug Discovery<\/p>\n<p>28 |\u00a0<b>Bianka Holguin<\/b> Mutations in Small Heat-Shock Protein 27 Affect Phosphorylation Regulated Chaperone Activity<\/p>\n<p>29 |\u00a0<b>Lauren Jackson<\/b> Architecture of Mammalian Retromer by Single Particle Cryo-EM<\/p>\n<p>30 |\u00a0<b>Michael Sheedlo<\/b> Cryo-EM Analysis of the TcdB-Frizzled-2 Interaction<\/p>\n<p>31 |\u00a0<b>Heather Kroh<\/b> <i>Clostridium difficile<\/i>\u00a0Toxin TcdB Bound to Bezlotoxumab F(ab\u2019)2 Reveals a Distinct Conformation that May Influence Toxin Neutralization<\/p>\n<p>32 |\u00a0<b>Andrei\u00a0 Fokine<\/b> Tomogram Averaging using a Locked Self-Rotation Function<\/p>\n<p>33 |\u00a0<b>Perla A. Pena Palomino<\/b> Role of C1QL3 as a Synaptic Organizer in Specific Subsets of Neurons in Brain: Structural Studies of C1QL-Mediated Complexes<\/p>\n<p>34 |\u00a0<b>Brenda Gonzalez<\/b>\u00a0Virtual Reality Training Tools for Cryo-EM<\/p>\n","protected":false},"excerpt":{"rendered":"<p>Posters will be displayed on Wednesday, November 7th, 2018 from 4:00pm\u00a0\u2014 5:00pm. If you are presenting, we ask that you\u00a0setup from anytime before 4:00pm on\u00a0Wednesday. You may leave the posters setup until the end of the day. 1 |\u00a0Nestor Zaluzec Soft Matter and Biosystems \u00a0Microanalysis by Analytical Electron Microscopy 2 |\u00a0\u00a0Ziao Fu The Structural Basis [&hellip;]<\/p>\n","protected":false},"author":3,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"_acf_changed":false,"footnotes":""},"class_list":["post-535","page","type-page","status-publish","hentry","post-preview"],"acf":[],"_links":{"self":[{"href":"https:\/\/www.purdue.edu\/cryoem2018\/wp-json\/wp\/v2\/pages\/535","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/www.purdue.edu\/cryoem2018\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/www.purdue.edu\/cryoem2018\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/www.purdue.edu\/cryoem2018\/wp-json\/wp\/v2\/users\/3"}],"replies":[{"embeddable":true,"href":"https:\/\/www.purdue.edu\/cryoem2018\/wp-json\/wp\/v2\/comments?post=535"}],"version-history":[{"count":3,"href":"https:\/\/www.purdue.edu\/cryoem2018\/wp-json\/wp\/v2\/pages\/535\/revisions"}],"predecessor-version":[{"id":560,"href":"https:\/\/www.purdue.edu\/cryoem2018\/wp-json\/wp\/v2\/pages\/535\/revisions\/560"}],"wp:attachment":[{"href":"https:\/\/www.purdue.edu\/cryoem2018\/wp-json\/wp\/v2\/media?parent=535"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}