9TBE
Cryo-EM structure of the light-driven sodium pump ErNaR in the monomeric form in the K2 state
Summary for 9TBE
| Entry DOI | 10.2210/pdb9tbe/pdb |
| Related | 9TBD 9TBF |
| EMDB information | 55761 55765 55766 55769 |
| Descriptor | Bacteriorhodopsin-like protein, EICOSANE, DODECYL-BETA-D-MALTOSIDE, ... (5 entities in total) |
| Functional Keywords | rhodopsin, ernar, sodium pump, phototransduction, membrane protein |
| Biological source | Erythrobacter |
| Total number of polymer chains | 1 |
| Total formula weight | 34946.02 |
| Authors | Haubner, M.,Williams, H.M.,Hruby, J.,Straub, M.S.,Guskov, A.,Kovalev, K.,Drabbels, M.,Lorenz, U.J. (deposition date: 2025-11-19, release date: 2025-12-17) |
| Primary citation | Haubner, M.,Williams, H.M.,Hruby, J.,Straub, M.S.,Guskov, A.,Kovalev, K.,Drabbels, M.,Lorenz, U.J. Microsecond Time-Resolved Cryo-EM Based on Jet Vitrification. Biorxiv, 2025 Cited by PubMed Abstract: 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 μs. This allows us to observe the photoinduced dynamics of the light-driven sodium pump NaR on the microsecond to millisecond timescale. Our experiments significantly expand the ability of cryo-EM to observe protein dynamics across multiple timescales. PubMed: 41332690DOI: 10.1101/2025.11.21.689681 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.8 Å) |
Structure validation
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