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Open Access Publications from the University of California

Coherent diffractive imaging of microtubules using an X-ray laser.

  • Author(s): 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 MG
  • 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
  • et al.

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.

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