Corrigendum to "A dose-rate effect in single-particle electron microscopy" [J. Struct. Biol. 161 (2008) 92-100] (DOI:10.1016/j.jsb.2007.09.017);A dose-rate effect in single-particle electron microscopy

Journal of Structural Biology

Volumn 161, Issue 1, 2008, Pages 92-100

  Chen, James Z ^a   Sachse, Carsten ^a,b   Xu, Chen ^a   Mielke, Thorsten ^c   Spahn, Christian M T ^d   Grigorieff, Nikolaus ^a  

^a BRANDEIS UNIVERSITY   (United States)

^b FRITZ LIPMANN INSTITUTE   (Germany)

^c MAX PLANCK INSTITUTE FOR MOLECULAR GENETICS   (Germany)

^d CHARITÉ UNIVERSITÄTSMEDIZIN BERLIN   (Germany)

Author keywords

Beam induced movement; Dose rate effect; High resolution EM; Radiation damage; Single particle electron cryo microscopy

Indexed keywords

ARTICLE; CRYOELECTRON MICROSCOPY; ELECTRON BEAM; ELECTRON MICROSCOPY; FOURIER TRANSFORMATION; IMAGE ANALYSIS; IMAGE QUALITY; IMAGING SYSTEM; MACROMOLECULE; PRIORITY JOURNAL; PROTEIN STRUCTURE; RADIATION INJURY; TECHNIQUE; TOBACCO MOSAIC VIRUS;

EID: 37349002528     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2008.08.001     Document Type: Erratum

References (22)

1. Brink J., Sherman M.B., Berriman J., and Chiu W. Evaluation of charging on macromolecules in electron cryomicroscopy. Ultramicroscopy 72 (1998) 41-52
2. Carragher B., Kisseberth N., Kriegman D., Milligan R.A., Potter C.S., Pulokas J., and Reilein A. Leginon: an automated system for acquisition of images from vitreous ice specimens. J. Struct. Biol. 132 (2000) 33-45
3. Chen J.Z., and Grigorieff N. SIGNATURE: a single-particle selection system for molecular electron microscopy. J. Struct. Biol. 157 (2007) 168-173
4. Cosslett V.E. Radiation damage in the high resolution electron microscopy of biological materials: a review. J. Microsc. 113 (1978) 113-129
5. Downing K.H., and Glaeser R.M. Improvement in high resolution image quality of radiation-sensitive specimens achieved with reduced spot size of the electron beam. Ultramicroscopy 20 (1986) 269-278
6. Dubochet J., Lepault J., Freeman R., Berriman J.A., and Homo J.C. Electron microscopy of frozen water and aqueous solutions. J. Microsc. 128 (1982) 219-237
7. Dubochet J., Adrian M., Chang J.J., Homo J.C., Lepault J., McDowall A.W., and Schultz P. Cryo-electron microscopy of vitrified specimens. Quart. Rev. Biophys. 21 (1988) 129-228
8. Frank J. Single-particle imaging of macromolecules by cryo-electron microscopy. Annu. Rev. Biophys. Biolol. Struct. 31 (2002) 303-319
9. Glaeser R.M., and Taylor K.A. Radiation damage relative to transmission electron microscopy of biological specimens at low temperature: a review. J. Microsc. 112 (1978) 127-138
10. Grigorieff N. Three-dimensional structure of bovine NADH: ubiquinone oxidoreductase (complex I) at 22 Å in ice. J. Mol. Biol. 277 (1998) 1033-1046
11. Henderson R. Image contrast in high-resolution electron microscopy of biological macromolecules: TMV in ice. Ultramicroscopy 46 (1992) 1-18
12. Iancu C.V., Wright E.R., Heymann J.B., and Jensen G.J. A comparison of liquid nitrogen and liquid helium as cryogens for electron cryotomography. J. Struct. Biol. 153 (2006) 231-240
13. Leapman R.D., and Sun S. Cryo-electron energy loss spectroscopy: observations on vitrified hydrated specimens and radiation damage. Ultramicroscopy 59 (1995) 71-79
14. Leschziner A.E., and Nogales E. The orthogonal tilt reconstruction method: An approach to generating single-class volumes with no missing cone for ab initio reconstruction of asymmetric particles. J. Struct. Biol. 153 (2006) 284-299
15. Misra M., and Egerton R.F. Assessment of electron irradiation damage to biomolecules by electron diffraction and electron energy-loss spectroscopy. Ultramicroscopy 15 (1984) 337-343
16. Murray J., and Garman E. Investigation of possible free-radical scavengers and metrics for radiation damage in protein cryocrystallography. J. Synchrotron Radiat. 9 (2002) 347-354
17. Namba K., Pattanayek R., and Stubbs G. Visualization of protein-nucleic acid interactions in a virus. Refined structure of intact tobacco mosaic virus at 2.9 Å resolution by X-ray fiber diffraction. J. Mol. Biol. 208 (1989) 307-325
18. Radermacher M., Wagenknecht T., Verschoor A., and Frank J. Three-dimensional reconstruction from a single-exposure, random conical tilt series applied to the 50 S ribosomal subunit of Escherichia coli. J. Microsc. 146 (1987) 113-136
19. Ravelli R., and Garman E.F. Radiation damage in macromolecular cryocrystallography. Curr. Opin. Struct. Biol. 16 (2006) 624-629
20. Sachse C., Chen J.Z., Coureux P., Stroupe M.E., Fandrich M., and Grigorieff N. High-resolution electron microscopy of helical specimens: a fresh look at tobacco mosaic virus. J. Mol. Biol. 371 (2007) 812-835
21. Taylor K.A., and Glaeser R.M. Electron microscopy of frozen hydrated biological specimens. J. Ultrastruct. Res. 55 (1976) 448-456
22. Typke D., Gilpin C.J., Downing K.H., and Glaeser R.M. Stroboscopic image capture: reducing the dose per frame by a factor of 30 does not prevent beam-induced specimen movement in paraffin. Ultramicroscopy 107 (2007) 106-115