View source for 9tbd


==Cryo-EM structure of the light-driven sodium pump ErNaR in the pentameric form==
<StructureSection load='9tbd' size='340' side='right'caption='[[9tbd]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9tbd]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Erythrobacter Erythrobacter]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9TBD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9TBD FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene>, <scene name='pdbligand=LFA:EICOSANE'>LFA</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=RET:RETINAL'>RET</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9tbd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9tbd OCA], [https://pdbe.org/9tbd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9tbd RCSB], [https://www.ebi.ac.uk/pdbsum/9tbd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9tbd ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Understanding and ultimately predicting the function of proteins is one of the frontiers in structural biology. This will only be possible if it becomes feasible to routinely observe proteins on the fast timescales on which they perform their tasks. Recently, laser flash melting and revitrification experiments have improved the time resolution of cryo-electron microscopy (cryo-EM) to microseconds, rendering it fast enough to observe the domain motions of proteins that are frequently linked to function. However, observations have been limited to a time window of just a few hundred microseconds. Here, we introduce time-resolved cryo-EM experiments based on jet vitrification that combine microsecond resolution with an observation window of up to seconds. We use a short laser pulse to initiate protein dynamics, and as they unfold, vitrify the sample with a jet of a liquid cryogen to arrest the dynamics at that point in time. We demonstrate that our approach affords near-atomic spatial resolution and a time resolution of 21 micros. This allows us to observe the photoinduced dynamics of the light-driven sodium pump Er NaR on the microsecond to millisecond timescale. Our experiments significantly expand the ability of cryo-EM to observe protein dynamics across multiple timescales.

Microsecond Time-Resolved Cryo-EM Based on Jet Vitrification.,Haubner M, Williams HM, Hruby J, Straub MS, Guskov A, Kovalev K, Drabbels M, Lorenz UJ bioRxiv [Preprint]. 2025 Nov 21:2025.11.21.689681. doi: , 10.1101/2025.11.21.689681. PMID:41332690<ref>PMID:41332690</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9tbd" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Erythrobacter]]
[[Category: Large Structures]]
[[Category: Drabbels M]]
[[Category: Guskov A]]
[[Category: Haubner M]]
[[Category: Hruby J]]
[[Category: Kovalev K]]
[[Category: Lorenz UJ]]
[[Category: Straub MS]]
[[Category: Williams HM]]