Literature DB >> 30242932

On the damage done to the structure of the Thermoplasma acidophilum proteasome by electron radiation.

Jimin Wang1, Zheng Liu2,3, Robert H Crabtree4, Joachim Frank2,5, Peter B Moore1,4.   

Abstract

It has long been known that proteins are damaged when they are exposed to the electron beam in an electron microscope. Here we show that exposure to electrons under cryo-EM conditions leads to a small change in the quaternary structure of the Thermoplasma acidophilum proteasome, and that backbones atoms belonging to the α-helices in this molecule appear to be particular prone to chemical damage. A chemical mechanism is proposed for this damage. Both this local chemical effect and the more global quaternary structure effect appear to heterogenize samples leading to a radiation dose-dependent degradation of the resolution of the EM maps obtained from this molecule.
© 2018 The Protein Society.

Entities:  

Keywords:  cryo-electron microscopy; difference Fourier method; electron radiation-induced damage; proteasome

Mesh:

Substances:

Year:  2018        PMID: 30242932      PMCID: PMC6237698          DOI: 10.1002/pro.3511

Source DB:  PubMed          Journal:  Protein Sci        ISSN: 0961-8368            Impact factor:   6.725


  30 in total

1.  The Calpha ---H...O hydrogen bond: a determinant of stability and specificity in transmembrane helix interactions.

Authors:  A Senes; I Ubarretxena-Belandia; D M Engelman
Journal:  Proc Natl Acad Sci U S A       Date:  2001-07-31       Impact factor: 11.205

2.  Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy.

Authors:  Peter B Rosenthal; Richard Henderson
Journal:  J Mol Biol       Date:  2003-10-31       Impact factor: 5.469

3.  Oxygen additions in serial femtosecond crystallographic protein structures.

Authors:  Jimin Wang
Journal:  Protein Sci       Date:  2016-07-26       Impact factor: 6.725

4.  Shoot-and-Trap: use of specific x-ray damage to study structural protein dynamics by temperature-controlled cryo-crystallography.

Authors:  Jacques-Philippe Colletier; Dominique Bourgeois; Benoît Sanson; Didier Fournier; Joel L Sussman; Israel Silman; Martin Weik
Journal:  Proc Natl Acad Sci U S A       Date:  2008-08-13       Impact factor: 11.205

Review 5.  Direct Electron Detectors.

Authors:  G McMullan; A R Faruqi; R Henderson
Journal:  Methods Enzymol       Date:  2016-07-05       Impact factor: 1.600

Review 6.  Single-Particle Cryo-EM at Crystallographic Resolution.

Authors:  Yifan Cheng
Journal:  Cell       Date:  2015-04-23       Impact factor: 41.582

7.  RELION: implementation of a Bayesian approach to cryo-EM structure determination.

Authors:  Sjors H W Scheres
Journal:  J Struct Biol       Date:  2012-09-19       Impact factor: 2.867

8.  Cryo-EM single particle analysis with the Volta phase plate.

Authors:  Radostin Danev; Wolfgang Baumeister
Journal:  Elife       Date:  2016-03-07       Impact factor: 8.140

9.  CryoEM at IUCrJ: a new era.

Authors:  Sriram Subramaniam; Werner Kühlbrandt; Richard Henderson
Journal:  IUCrJ       Date:  2016-01-01       Impact factor: 4.769

10.  Microscopic charge fluctuations cause minimal contrast loss in cryoEM.

Authors:  Christopher J Russo; Richard Henderson
Journal:  Ultramicroscopy       Date:  2018-01-31       Impact factor: 2.689

View more
  1 in total

1.  High-resolution cryo-EM structure of photosystem II reveals damage from high-dose electron beams.

Authors:  Koji Kato; Naoyuki Miyazaki; Tasuku Hamaguchi; Yoshiki Nakajima; Fusamichi Akita; Koji Yonekura; Jian-Ren Shen
Journal:  Commun Biol       Date:  2021-03-22
  1 in total

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