Literature DB >> 10966635

Conformational changes studied by cryo-electron microscopy.

H R Saibil1.   

Abstract

Biological processes involving movement, such as muscle contraction or the opening of an ion channel through a membrane, are mediated through conformational changes. These changes often occur in large and flexible macromolecular complexes. Cryo-electron microscopy provides a means of capturing different conformational states of such assemblies. Even if the resulting density maps are at low resolution, they can be combined with atomic structures of subcomplexes or isolated components determined by X-ray crystallography or NMR. This review presents a brief summary of the principles and recent advances in macromolecular structure determination by cryo-electron microscopy.

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Year:  2000        PMID: 10966635     DOI: 10.1038/78923

Source DB:  PubMed          Journal:  Nat Struct Biol        ISSN: 1072-8368


  23 in total

Review 1.  Chaperonin 60 unfolds its secrets of cellular communication.

Authors:  Maria Maguire; Anthony R M Coates; Brian Henderson
Journal:  Cell Stress Chaperones       Date:  2002-10       Impact factor: 3.667

2.  Normal mode-based fitting of atomic structure into electron density maps: application to sarcoplasmic reticulum Ca-ATPase.

Authors:  Konrad Hinsen; Nathalie Reuter; Jorge Navaza; David L Stokes; Jean-Jacques Lacapère
Journal:  Biophys J       Date:  2004-11-12       Impact factor: 4.033

3.  Accurate flexible fitting of high-resolution protein structures to small-angle x-ray scattering data using a coarse-grained model with implicit hydration shell.

Authors:  Wenjun Zheng; Mustafa Tekpinar
Journal:  Biophys J       Date:  2011-12-20       Impact factor: 4.033

Review 4.  Single particle analysis: a new approach to solving the 3D structure of myosin filaments.

Authors:  Hind A Al-Khayat; Edward P Morris; John M Squire
Journal:  J Muscle Res Cell Motil       Date:  2005-02-24       Impact factor: 2.698

5.  Can conformational change be described by only a few normal modes?

Authors:  Paula Petrone; Vijay S Pande
Journal:  Biophys J       Date:  2005-12-16       Impact factor: 4.033

6.  Normal-mode flexible fitting of high-resolution structure of biological molecules toward one-dimensional low-resolution data.

Authors:  Christian Gorba; Osamu Miyashita; Florence Tama
Journal:  Biophys J       Date:  2007-11-09       Impact factor: 4.033

7.  Protein structure fitting and refinement guided by cryo-EM density.

Authors:  Maya Topf; Keren Lasker; Ben Webb; Haim Wolfson; Wah Chiu; Andrej Sali
Journal:  Structure       Date:  2008-02       Impact factor: 5.006

8.  Analyzing protein dynamics using hydrogen exchange mass spectrometry.

Authors:  Nikolai Hentze; Matthias P Mayer
Journal:  J Vis Exp       Date:  2013-11-29       Impact factor: 1.355

9.  Consensus among flexible fitting approaches improves the interpretation of cryo-EM data.

Authors:  Aqeel Ahmed; Paul C Whitford; Karissa Y Sanbonmatsu; Florence Tama
Journal:  J Struct Biol       Date:  2011-10-13       Impact factor: 2.867

10.  Flexible fitting of high-resolution x-ray structures into cryoelectron microscopy maps using biased molecular dynamics simulations.

Authors:  Marek Orzechowski; Florence Tama
Journal:  Biophys J       Date:  2008-10-10       Impact factor: 4.033

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