Unknown

Dataset Information

0

Diffracted X-ray Blinking Tracks Single Protein Motions.


ABSTRACT: Single molecule dynamics studies have begun to use quantum probes. Single particle analysis using cryo-transmission electron microscopy has dramatically improved the resolution when studying protein structures and is shifting towards molecular motion observations. X-ray free-electron lasers are also being explored as routes for determining single molecule structures of biological entities. Here, we propose a new X-ray single molecule technology that allows observation of molecular internal motion over long time scales, ranging from milliseconds up to 103?seconds. Our method uses both low-dose monochromatic X-rays and nanocrystal labelling technology. During monochromatic X-ray diffraction experiments, the intensity of X-ray diffraction from moving single nanocrystals appears to blink because of Brownian motion in aqueous solutions. X-ray diffraction spots from moving nanocrystals were observed to cycle in and out of the Bragg condition. Consequently, the internal motions of a protein molecule labelled with nanocrystals could be extracted from the time trajectory using this diffracted X-ray blinking (DXB) approach. Finally, we succeeded in distinguishing the degree of fluctuation motions of an individual acetylcholine-binding protein (AChBP) interacting with acetylcholine (ACh) using a laboratory X-ray source.

SUBMITTER: Sekiguchi H 

PROVIDER: S-EPMC6269541 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature

altmetric image

Publications


Single molecule dynamics studies have begun to use quantum probes. Single particle analysis using cryo-transmission electron microscopy has dramatically improved the resolution when studying protein structures and is shifting towards molecular motion observations. X-ray free-electron lasers are also being explored as routes for determining single molecule structures of biological entities. Here, we propose a new X-ray single molecule technology that allows observation of molecular internal motio  ...[more]

Similar Datasets

| S-EPMC7935957 | biostudies-literature
| S-EPMC8270646 | biostudies-literature
| S-EPMC5831586 | biostudies-literature
| S-EPMC7062842 | biostudies-literature
| S-EPMC4759603 | biostudies-other
| S-EPMC523450 | biostudies-literature
| S-EPMC5947722 | biostudies-literature
| S-EPMC3170728 | biostudies-literature
| S-EPMC4354043 | biostudies-literature
| S-EPMC2698891 | biostudies-literature