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TitleVitroJet: new features and case studies.
Journal, issue, pagesActa Crystallogr D Struct Biol, Vol. 80, Issue Pt 4, Page 232-246, Year 2024
Publish dateApr 1, 2024
AuthorsRene J M Henderikx / Daniel Mann / Aušra Domanska / Jing Dong / Saba Shahzad / Behnam Lak / Aikaterini Filopoulou / Damian Ludig / Martin Grininger / Jeffrey Momoh / Elina Laanto / Hanna M Oksanen / Kyrylo Bisikalo / Pamela A Williams / Sarah J Butcher / Peter J Peters / Bart W A M M Beulen /
PubMed AbstractSingle-particle cryo-electron microscopy has become a widely adopted method in structural biology due to many recent technological advances in microscopes, detectors and image processing. Before ...Single-particle cryo-electron microscopy has become a widely adopted method in structural biology due to many recent technological advances in microscopes, detectors and image processing. Before being able to inspect a biological sample in an electron microscope, it needs to be deposited in a thin layer on a grid and rapidly frozen. The VitroJet was designed with this aim, as well as avoiding the delicate manual handling and transfer steps that occur during the conventional grid-preparation process. Since its creation, numerous technical developments have resulted in a device that is now widely utilized in multiple laboratories worldwide. It features plasma treatment, low-volume sample deposition through pin printing, optical ice-thickness measurement and cryofixation of pre-clipped Autogrids through jet vitrification. This paper presents recent technical improvements to the VitroJet and the benefits that it brings to the cryo-EM workflow. A wide variety of applications are shown: membrane proteins, nucleosomes, fatty-acid synthase, Tobacco mosaic virus, lipid nanoparticles, tick-borne encephalitis viruses and bacteriophages. These case studies illustrate the advancement of the VitroJet into an instrument that enables accurate control and reproducibility, demonstrating its suitability for time-efficient cryo-EM structure determination.
External linksActa Crystallogr D Struct Biol / PubMed:38488730 / PubMed Central
MethodsEM (single particle) / EM (helical sym.)
Resolution3.3 - 5.4 Å
Structure data

EMDB-19477: Saccharomyces cerevisiae FAS type I
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-19489: Tobacco mosaic virus from scanning transmission electron microscopy at CSA=2.0 mrad
Method: EM (helical sym.) / Resolution: 5.4 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)

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