Journal
JOURNAL OF SYNCHROTRON RADIATION
Volume 24, Issue -, Pages 727-737Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1600577517007767
Keywords
three-dimensional reconstruction; single-particle analysis; X-ray free-electron laser; coherent X-ray diffraction imaging
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Funding
- FOCUS for Establishing Supercomputing Center of Excellence
- JSPS KAKENHI [16K05527]
- Grants-in-Aid for Scientific Research [16K05527] Funding Source: KAKEN
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The three-dimensional (3D) structural analysis of single particles using an X-ray free-electron laser (XFEL) is a new structural biology technique that enables observations of molecules that are difficult to crystallize, such as flexible biomolecular complexes and living tissue in the state close to physiological conditions. In order to restore the 3D structure from the diffraction patterns obtained by the XFEL, computational algorithms are necessary as the orientation of the incident beam with respect to the sample needs to be estimated. A program package for XFEL single-particle analysis based on the Xmipp software package, that is commonly used for image processing in 3D cryo-electron microscopy, has been developed. The reconstruction program has been tested using diffraction patterns of an aerosol nanoparticle obtained by tomographic coherent X-ray diffraction microscopy.
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