scholarly journals Author response: 2.8 Å resolution reconstruction of the Thermoplasma acidophilum 20S proteasome using cryo-electron microscopy

2015 ◽  
Author(s):  
Melody G Campbell ◽  
David Veesler ◽  
Anchi Cheng ◽  
Clinton S Potter ◽  
Bridget Carragher
Keyword(s):  
Electron Microscopy ◽  
Author Response ◽  
20S Proteasome ◽  
Thermoplasma Acidophilum ◽  
Cryo Electron Microscopy

scholarly journals 2.8 Å resolution reconstruction of the Thermoplasma acidophilum 20S proteasome using cryo-electron microscopy

eLife ◽  
2015 ◽  
Vol 4 ◽  
Author(s):  
Melody G Campbell ◽  
David Veesler ◽  
Anchi Cheng ◽  
Clinton S Potter ◽  
Bridget Carragher
Keyword(s):  
Electron Microscopy ◽  
Drug Design ◽  
Single Particle ◽  
Protein Structures ◽  
Rational Drug Design ◽  
20S Proteasome ◽  
Thermoplasma Acidophilum ◽  
Structure Based Drug Design ◽  
Cryo Electron Microscopy ◽  
Pharmaceutical Industries

Recent developments in detector hardware and image-processing software have revolutionized single particle cryo-electron microscopy (cryoEM) and led to a wave of near-atomic resolution (typically ∼3.3 Å) reconstructions. Reaching resolutions higher than 3 Å is a prerequisite for structure-based drug design and for cryoEM to become widely interesting to pharmaceutical industries. We report here the structure of the 700 kDa Thermoplasma acidophilum 20S proteasome (T20S), determined at 2.8 Å resolution by single-particle cryoEM. The quality of the reconstruction enables identifying the rotameric conformation adopted by some amino-acid side chains (rotamers) and resolving ordered water molecules, in agreement with the expectations for crystal structures at similar resolutions. The results described in this manuscript demonstrate that single particle cryoEM is capable of competing with X-ray crystallography for determination of protein structures of suitable quality for rational drug design.

scholarly journals Structure of the Blm10-20S Proteasome Complex by Single Particle Cryo Electron Microscopy

2006 ◽  
Vol 12 (S02) ◽  
pp. 372-373
Author(s):  
J Ortega ◽  
J Iwanczyk ◽  
K Sadre-Bazzaz ◽  
K Ferrell ◽  
E Kondrashkina ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Single Particle ◽  
20S Proteasome ◽  
Cryo Electron Microscopy

Extended abstract of a paper presented at Microscopy and Microanalysis 2006 in Chicago, Illinois, USA, July 30 – August 3, 2006

scholarly journals Author response: Molecular dynamics-based refinement and validation for sub-5 Å cryo-electron microscopy maps

2016 ◽  
Author(s):  
Abhishek Singharoy ◽  
Ivan Teo ◽  
Ryan McGreevy ◽  
John E Stone ◽  
Jianhua Zhao ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Molecular Dynamics ◽  
Author Response ◽  
Cryo Electron Microscopy

scholarly journals Author response: Structure of the human epithelial sodium channel by cryo-electron microscopy

2018 ◽  
Author(s):  
Sigrid Noreng ◽  
Arpita Bharadwaj ◽  
Richard Posert ◽  
Craig Yoshioka ◽  
Isabelle Baconguis
Keyword(s):  
Electron Microscopy ◽  
Sodium Channel ◽  
Epithelial Sodium Channel ◽  
Author Response ◽  
Cryo Electron Microscopy

scholarly journals Author response: Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy

2019 ◽  
Author(s):  
Ricardo Guerrero-Ferreira ◽  
Nicholas MI Taylor ◽  
Ana-Andreea Arteni ◽  
Pratibha Kumari ◽  
Daniel Mona ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Alpha Synuclein ◽  
Full Length ◽  
Author Response ◽  
Cryo Electron Microscopy

New challenges to image processing posed by cryo-Electron microscopy of single particles

1991 ◽  
Vol 49 ◽  
pp. 422-423
Author(s):  
Joachim Frank
Keyword(s):  
Electron Microscopy ◽  
Phase Contrast ◽  
Particle Orientation ◽  
Single Particles ◽  
Contrast Transfer Function ◽  
Virtual Absence ◽  
Cryo Electron Microscopy ◽  
Spatial Frequencies ◽  
New Challenges ◽  
Particle Images

Compared with images of negatively stained single particle specimens, those obtained by cryo-electron microscopy have the following new features: (a) higher “signal” variability due to a higher variability of particle orientation; (b) reduced signal/noise ratio (S/N); (c) virtual absence of low-spatial-frequency information related to elastic scattering, due to the properties of the phase contrast transfer function (PCTF); and (d) reduced resolution due to the efforts of the microscopist to boost the PCTF at low spatial frequencies, in his attempt to obtain recognizable particle images.

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