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 - Funding Information:
Use of the Linac Coherent Light Source (LCLS), SLAC National Accelerator Laboratory, is supported by the U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences under Contract No. DE-AC02-76SF00515. Parts of the sample delivery system used at LCLS for this research was funded by the NIH Grant P41GM103393, formerly P41RR001209. We acknowledge SAXS beamtime at beamline I911-4 on the MAX II storage ring of the MAX IV Laboratory (formerly MAX-lab) and support by Dr Tomas Plivelic. We thank Fredrik Bråtner at Dalsjöfors Kött for providing us with calves’ brains. We are grateful to Dr Gregory Stewart at SLAC National Accelerator Laboratory for help with preparing Fig. 1. R.N. acknowledges funding from the Knut and Alice Wallenberg Foundation (Grant Numbers KAW 2012.0284, KAW 2012.0275 and KAW 2014.0275), the Swedish Research Council (Grant Numbers 2015-00560 and 349-2011-6485) and the Swedish Foundation for Strategic Research (Grant Number SRL10-0036). We are grateful for support from the Helmholtz Association through project-oriented funds to DESY. R.C.R. was supported by A*STAR (Agency for Science, Technology and Research), Singapore. PHZ was supported by the National Institutes of Health (NIH) under Award R01GM109019.
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 -