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Analysis of Global and Site-Specific Radiation Damage in Cryo-EM.

Hattne J, Shi D, Glynn C, Zee CT, Gallagher-Jones M, Martynowycz MW, Rodriguez JA, Gonen T
Structure 26 759-766.e4 (2018)
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Cited: 85 times
EuropePMC logo PMID: 29706530

Abstract

Micro-crystal electron diffraction (MicroED) combines the efficiency of electron scattering with diffraction to allow structure determination from nano-sized crystalline samples in cryoelectron microscopy (cryo-EM). It has been used to solve structures of a diverse set of biomolecules and materials, in some cases to sub-atomic resolution. However, little is known about the damaging effects of the electron beam on samples during such measurements. We assess global and site-specific damage from electron radiation on nanocrystals of proteinase K and of a prion hepta-peptide and find that the dynamics of electron-induced damage follow well-established trends observed in X-ray crystallography. Metal ions are perturbed, disulfide bonds are broken, and acidic side chains are decarboxylated while the diffracted intensities decay exponentially with increasing exposure. A better understanding of radiation damage in MicroED improves our assessment and processing of all types of cryo-EM data.

Articles - 6cll mentioned but not cited (1)

  1. Analysis of Global and Site-Specific Radiation Damage in Cryo-EM. Hattne J, Shi D, Glynn C, Zee CT, Gallagher-Jones M, Martynowycz MW, Rodriguez JA, Gonen T. Structure 26 759-766.e4 (2018)


Reviews citing this publication (17)

  1. Challenges and opportunities in cryo-EM single-particle analysis. Lyumkis D. J Biol Chem 294 5181-5197 (2019)
  2. The cryo-EM method microcrystal electron diffraction (MicroED). Nannenga BL, Gonen T. Nat Methods 16 369-379 (2019)
  3. CryoEM maps are full of potential. Marques MA, Purdy MD, Yeager M. Curr Opin Struct Biol 58 214-223 (2019)
  4. MicroED in natural product and small molecule research. Danelius E, Halaby S, van der Donk WA, Gonen T. Nat Prod Rep 38 423-431 (2021)
  5. Beyond protein structure determination with MicroED. Nguyen C, Gonen T. Curr Opin Struct Biol 64 51-58 (2020)
  6. The complementarity of serial femtosecond crystallography and MicroED for structure determination from microcrystals. Zatsepin NA, Li C, Colasurd P, Nannenga BL. Curr Opin Struct Biol 58 286-293 (2019)
  7. Electron Diffraction of 3D Molecular Crystals. Saha A, Nia SS, Rodríguez JA. Chem Rev 122 13883-13914 (2022)
  8. Metalloprotein catalysis: structural and mechanistic insights into oxidoreductases from neutron protein crystallography. Schröder GC, Meilleur F. Acta Crystallogr D Struct Biol 77 1251-1269 (2021)
  9. An Overview of Microcrystal Electron Diffraction (MicroED). Mu X, Gillman C, Nguyen C, Gonen T. Annu Rev Biochem 90 431-450 (2021)
  10. Cryo-electron tomography related radiation-damage parameters for individual-molecule 3D structure determination. Xue H, Zhang M, Liu J, Wang J, Ren G. Front Chem 10 889203 (2022)
  11. Macromolecular crystallography using microcrystal electron diffraction. Clabbers MTB, Xu H. Acta Crystallogr D Struct Biol 77 313-324 (2021)
  12. MicroED: conception, practice and future opportunities. Clabbers MTB, Shiriaeva A, Gonen T. IUCrJ 9 169-179 (2022)
  13. The Evolution and the Advantages of MicroED. Nannenga BL, Bu G, Shi D. Front Mol Biosci 5 114 (2018)
  14. Growing and making nano- and microcrystals. Shoeman RL, Hartmann E, Schlichting I. Nat Protoc 18 854-882 (2023)
  15. MicroED for the study of protein-ligand interactions and the potential for drug discovery. Clark LJ, Bu G, Nannenga BL, Gonen T. Nat Rev Chem 5 853-858 (2021)
  16. Analysis and comparison of electron radiation damage assessments in Cryo-EM by single particle analysis and micro-crystal electron diffraction. Shi D, Huang R. Front Mol Biosci 9 988928 (2022)
  17. Coming of Age: Cryo-Electron Tomography as a Versatile Tool to Generate High-Resolution Structures at Cellular/Biological Interfaces. Wang Z, Zhang Q, Mim C. Int J Mol Sci 22 6177 (2021)

Articles citing this publication (67)



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