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TitleLight-coupled cryo-plunger for time-resolved cryo-EM.
Journal, issue, pagesJ Struct Biol, Vol. 212, Issue 3, Page 107624, Year 2020
Publish dateDec 1, 2020
AuthorsNate Yoder / Farzad Jalali-Yazdi / Sigrid Noreng / Alexandra Houser / Isabelle Baconguis / Eric Gouaux /
PubMed AbstractProteins are dynamic molecules that can undergo rapid conformational rearrangements in response to stimuli. These structural changes are often critical to protein function, and thus elucidating time- ...Proteins are dynamic molecules that can undergo rapid conformational rearrangements in response to stimuli. These structural changes are often critical to protein function, and thus elucidating time-dependent conformational landscapes has been a long-standing goal of structural biology. To harness the power of single particle cryo-EM methods to enable 'time-resolved' structure determination, we have developed a light-coupled cryo-plunger that pairs flash-photolysis of caged ligands with rapid sample vitrification. The 'flash-plunger' consists of a high-power ultraviolet LED coupled with focusing optics and a motorized linear actuator, enabling the user to immobilize protein targets in vitreous ice within a programmable time window - as short as tens of milliseconds - after stimulus delivery. The flash-plunger is a simple, inexpensive and flexible tool to explore short-lived conformational states previously unobtainable by conventional sample preparation methods.
External linksJ Struct Biol / PubMed:32950604 / PubMed Central
MethodsEM (single particle)
Resolution3.5 - 4.0 Å
Structure data

EMDB-21384:
Map of an acid-sensing ion channel in a desensitized state after photo-uncaging protons.
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-21385:
Map of an acid-sensing ion channel in a resting state at high pH.
Method: EM (single particle) / Resolution: 4.0 Å

Source
  • Gallus gallus (chicken)

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