TY - JOUR
T1 - Coherent diffractive imaging of microtubules using an X-ray laser
AU - Brändén, Gisela
AU - Hammarin, Greger
AU - Harimoorthy, Rajiv
AU - Johansson, Alexander
AU - Arnlund, David
AU - Malmerberg, Erik
AU - Barty, Anton
AU - Tångefjord, Stefan
AU - Berntsen, Peter
AU - DePonte, Daniel P.
AU - Seuring, Carolin
AU - White, Thomas A.
AU - Stellato, Francesco
AU - Bean, Richard
AU - Beyerlein, Kenneth R.
AU - Chavas, Leonard M.G.
AU - Fleckenstein, Holger
AU - Gati, Cornelius
AU - Ghoshdastider, Umesh
AU - Gumprecht, Lars
AU - Oberthür, Dominik
AU - Popp, David
AU - Seibert, Marvin
AU - Tilp, Thomas
AU - Messerschmidt, Marc
AU - Williams, Garth J.
AU - Loh, N. Duane
AU - Chapman, Henry N.
AU - Zwart, Peter
AU - Liang, Mengning
AU - Boutet, Sébastien
AU - Robinson, Robert C.
AU - Neutze, Richard
N1 - Publisher Copyright:
© 2019, The Author(s).
PY - 2019/12/1
Y1 - 2019/12/1
N2 - 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.
AB - 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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U2 - 10.1038/s41467-019-10448-x
DO - 10.1038/s41467-019-10448-x
M3 - Article
C2 - 31197138
AN - SCOPUS:85067364892
SN - 2041-1723
VL - 10
JO - Nature communications
JF - Nature communications
IS - 1
M1 - 2589
ER -