- Main
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.
Published Web Location
https://doi.org/10.1038/s41467-019-10448-xAbstract
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.