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Coherent diffractive imaging of microtubules using an X-ray laser

X-ray free electron lasers (XFELs) create new possibilities for structural studies of biological objects that extend beyond what is possible with synchrotron radiation. Serial femtosecond crystallography has allowed high-resolution structures to be determined from micro-meter sized crystals, whereas...

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Detalles Bibliográficos
Autores principales: Brändén, Gisela, Hammarin, Greger, Harimoorthy, Rajiv, Johansson, Alexander, Arnlund, David, Malmerberg, Erik, Barty, Anton, Tångefjord, Stefan, Berntsen, Peter, DePonte, Daniel P., Seuring, Carolin, White, Thomas A., Stellato, Francesco, Bean, Richard, Beyerlein, Kenneth R., Chavas, Leonard M. G., Fleckenstein, Holger, Gati, Cornelius, Ghoshdastider, Umesh, Gumprecht, Lars, Oberthür, Dominik, Popp, David, Seibert, Marvin, Tilp, Thomas, Messerschmidt, Marc, Williams, Garth J., Loh, N. Duane, Chapman, Henry N., Zwart, Peter, Liang, Mengning, Boutet, Sébastien, Robinson, Robert C., Neutze, Richard
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6565740/
https://www.ncbi.nlm.nih.gov/pubmed/31197138
http://dx.doi.org/10.1038/s41467-019-10448-x
Descripción
Sumario:X-ray free electron lasers (XFELs) create new possibilities for structural studies of biological objects that extend beyond what is possible with synchrotron radiation. Serial femtosecond crystallography has allowed high-resolution structures to be determined from micro-meter sized crystals, whereas single particle coherent X-ray imaging requires development to extend the resolution beyond a few tens of nanometers. Here we describe an intermediate approach: the XFEL imaging of biological assemblies with helical symmetry. We collected X-ray scattering images from samples of microtubules injected across an XFEL beam using a liquid microjet, sorted these images into class averages, merged these data into a diffraction pattern extending to 2 nm resolution, and reconstructed these data into a projection image of the microtubule. Details such as the 4 nm tubulin monomer became visible in this reconstruction. These results illustrate the potential of single-molecule X-ray imaging of biological assembles with helical symmetry at room temperature.