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6KJ2

200kV MicroED structure of FUS (37-42) SYSGYS solved from single crystal at 0.67 A

Summary for 6KJ2
Entry DOI10.2210/pdb6kj2/pdb
EMDB information0697
DescriptorRNA-binding protein FUS (2 entities in total)
Functional Keywordsfus, microed, ultrahigh resolution, rna binding protein
Biological sourceHomo sapiens (Human)
Total number of polymer chains1
Total formula weight662.65
Authors
Zhou, H.,Luo, F.,Luo, Z.,Li, D.,Liu, C.,Li, X. (deposition date: 2019-07-20, release date: 2019-10-02, Last modification date: 2024-03-27)
Primary citationZhou, H.,Luo, F.,Luo, Z.,Li, D.,Liu, C.,Li, X.
Programming Conventional Electron Microscopes for Solving Ultrahigh-Resolution Structures of Small and Macro-Molecules.
Anal.Chem., 91:10996-11003, 2019
Cited by
PubMed Abstract: Microcrystal electron diffraction (MicroED) is becoming a powerful tool in determining the crystal structures of biological macromolecules and small organic compounds. However, wide applications of this technique are still limited by the special requirement for radiation-tolerated movie-mode camera and the lack of automated data collection methods. Herein, we develop a stage-camera synchronization scheme to minimize the hardware requirements and enable the use of the conventional electron cryo-microscope with a single-frame CCD camera, which ensures not only the acquisition of ultrahigh-resolution diffraction data but also low cost in practice. This method renders the structure determination of both peptide and small organic compounds at ultrahigh resolution up to ∼0.60 Å with unambiguous assignment of nearly all hydrogen atoms. The present work provides a widely applicable solution for routine structure determination of MicroED and demonstrates the capability of the low-end 120 kV microscope with a CCD camera in solving ultrahigh resolution structures of both organic compounds and biological macromolecules.
PubMed: 31334636
DOI: 10.1021/acs.analchem.9b01162
PDB entries with the same primary citation
Experimental method
ELECTRON CRYSTALLOGRAPHY (0.67 Å)
Structure validation

227561

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