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TitleMicrosecond Time-Resolved Cryo-EM Based on Jet Vitrification.
Journal, issue, pagesbioRxiv, Year 2025
Publish dateNov 21, 2025
AuthorsMichal Haubner / Harry M Williams / Jakub Hruby / Monique S Straub / Albert Guskov / Kirill Kovalev / Marcel Drabbels / Ulrich J Lorenz /
PubMed AbstractUnderstanding 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 ...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.
External linksbioRxiv / PubMed:41332690 / PubMed Central
MethodsEM (single particle)
Resolution1.25 - 3.3 Å
Structure data

EMDB-55761: Cryo-EM map of mouse heavy chain apoferritin
Method: EM (single particle) / Resolution: 1.25 Å

55765

9tbd

EMDB-55765, PDB-9tbd:
Cryo-EM structure of the light-driven sodium pump ErNaR in the pentameric form
Method: EM (single particle) / Resolution: 2.1 Å

55766

9tbe

EMDB-55766, PDB-9tbe:
Cryo-EM structure of the light-driven sodium pump ErNaR in the monomeric form in the K2 state
Method: EM (single particle) / Resolution: 2.8 Å

55769

9tbf

EMDB-55769, PDB-9tbf:
Cryo-EM structure of the light-driven sodium pump ErNaR in the monomeric form in the O2 state
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-LFA:
EICOSANE

ChemComp-LMT:
DODECYL-BETA-D-MALTOSIDE / detergent*YM

ChemComp-RET:
RETINAL

ChemComp-HOH:
WATER

Source
  • Mus musculus (house mouse)
  • erythrobacter (bacteria)
KeywordsMEMBRANE PROTEIN / rhodopsin / ErNaR / sodium pump / phototransduction

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