Unknown

Dataset Information

0

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


ABSTRACT: 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.

SUBMITTER: Branden G 

PROVIDER: S-EPMC6565740 | biostudies-literature | 2019 Jun

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Brändén Gisela G   Hammarin Greger G   Harimoorthy Rajiv R   Johansson Alexander A   Arnlund David D   Malmerberg Erik E   Barty Anton A   Tångefjord Stefan S   Berntsen Peter P   DePonte Daniel P DP   Seuring Carolin C   White Thomas A TA   Stellato Francesco F   Bean Richard R   Beyerlein Kenneth R KR   Chavas Leonard M G LMG   Fleckenstein Holger H   Gati Cornelius C   Ghoshdastider Umesh U   Gumprecht Lars L   Oberthür Dominik D   Popp David D   Seibert Marvin M   Tilp Thomas T   Messerschmidt Marc M   Williams Garth J GJ   Loh N Duane ND   Chapman Henry N HN   Zwart Peter P   Liang Mengning M   Boutet Sébastien S   Robinson Robert C RC   Neutze Richard R  

Nature communications 20190613 1


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 assembl  ...[more]

Similar Datasets

| S-EPMC4643197 | biostudies-literature
| S-EPMC5431869 | biostudies-literature
| S-EPMC4547825 | biostudies-literature
| S-EPMC5940918 | biostudies-literature
| S-EPMC3724183 | biostudies-literature
| S-EPMC6370773 | biostudies-literature
| S-EPMC6503918 | biostudies-literature
| S-EPMC5377347 | biostudies-literature
| S-EPMC5574892 | biostudies-literature
| S-EPMC7206555 | biostudies-literature