Spectral DQE of the Volta phase plate

被引:22
作者
Buijsse, Bart [1 ]
Trompenaars, Piet [1 ]
Altin, Veli [1 ]
Danev, Radostin [2 ]
Glaeser, Robert M. [3 ]
机构
[1] Thermo Fisher Sci, Achtsweg Noord 5, NL-5651 GG Eindhoven, Netherlands
[2] Univ Tokyo, Grad Sch Med, Tokyo 1130033, Japan
[3] Univ Calif Berkeley, Lawrence Berkeley Natl Lab, Berkeley, CA 94705 USA
基金
美国国家卫生研究院; 日本科学技术振兴机构;
关键词
CRYO-EM STRUCTURE;
D O I
10.1016/j.ultramic.2020.113079
中图分类号
TH742 [显微镜];
学科分类号
摘要
The Volta Phase Plate (VPP) consists of a heated, thin film that is placed in the same plane as the focused diffraction pattern of an electron microscope. A change in surface potential develops at the point irradiated by the intense, unscattered electron beam, and this altered surface potential produces, in turn, a phase shift between the unscattered and scattered parts of the electron wave. While the VPP thus increases the image contrast for weak-phase objects at low spatial frequencies, we report here that it also leads to the loss of an increasing fraction of the signal at higher resolution. The approximately linear dependence (with increasing resolution) of this loss has been quantified at 200 kV and 300 kV, using evaporated-carbon films of different thicknesses as Volta phase plates. In all cases, the loss of signal remains almost independent of variation of the conditions and parameters that were tested. In spite of having done a number of additional, discovery-based experiments, the cause of this loss of signal remains unexplained at this point.
引用
收藏
页数:6
相关论文
共 17 条
[1]   A molecular census of 26S proteasomes in intact neurons [J].
Asano, Shoh ;
Fukuda, Yoshiyuki ;
Beck, Florian ;
Aufderheide, Antje ;
Foerster, Friedrich ;
Danev, Radostin ;
Baumeister, Wolfgang .
SCIENCE, 2015, 347 (6220) :439-442
[2]   Volta potential phase plate for in-focus phase contrast transmission electron microscopy [J].
Danev, Radostin ;
Buijsse, Bart ;
Khoshouei, Maryam ;
Plitzko, Juergen M. ;
Baumeister, Wolfgang .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2014, 111 (44) :15635-15640
[3]   Correction of high-resolution data for curvature of the Ewald sphere [J].
DeRosier, DJ .
ULTRAMICROSCOPY, 2000, 81 (02) :83-98
[5]   The structure of a prokaryotic viral envelope protein expands the landscape of membrane fusion proteins [J].
El Omari, Kamel ;
Li, Sai ;
Kotecha, Abhay ;
Walter, Thomas S. ;
Bignon, Eduardo A. ;
Harlos, Karl ;
Somerharju, Pentti ;
De Haas, Felix ;
Clare, Daniel K. ;
Molin, Mika ;
Hurtado, Felipe ;
Li, Mengqiu ;
Grimes, Jonathan M. ;
Bamford, Dennis H. ;
Tischler, Nicole D. ;
Huiskonen, Juha T. ;
Stuart, David I. ;
Roine, Elina .
NATURE COMMUNICATIONS, 2019, 10 (1)
[6]   Single particle cryo-EM reconstruction of 52 kDa streptavidin at 3.2 Angstrom resolution [J].
Fan, Xiao ;
Wang, Jia ;
Zhang, Xing ;
Yang, Zi ;
Zhang, Jin-Can ;
Zhao, Lingyun ;
Peng, Hai-Lin ;
Lei, Jianlin ;
Wang, Hong-Wei .
NATURE COMMUNICATIONS, 2019, 10 (1)
[7]   Breaking the spherical and chromatic aberration barrier in transmission electron microscopy [J].
Freitag, B ;
Kujawa, S ;
Mul, PM ;
Ringnalda, J ;
Tiemeijer, PC .
ULTRAMICROSCOPY, 2005, 102 (03) :209-214
[8]   Electron cryotomography of vitrified cells with a Volta phase plate [J].
Fukuda, Yoshiyuki ;
Laugks, Ulrike ;
Lucic, Vladan ;
Baumeister, Wolfgang ;
Danev, Radostin .
JOURNAL OF STRUCTURAL BIOLOGY, 2015, 190 (02) :143-154
[9]   Hole free phase plate tomography for materials sciences samples [J].
Hayashida, Misa ;
Cui, Kai ;
Najarian, Amin Morteza ;
McCreery, Richard ;
Jehanathan, Neerushana ;
Pawlowicz, Chris ;
Motoki, Sohei ;
Kawasaki, Masahiro ;
Konyuba, Yuji ;
Malac, Marek .
MICRON, 2019, 116 :54-60
[10]   High-resolution structure determination of sub-100 kDa complexes using conventional cryo-EM [J].
Herzik, Mark A., Jr. ;
Wu, Mengyu ;
Lander, Gabriel C. .
NATURE COMMUNICATIONS, 2019, 10 (1)