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The Structure of ClpB A Molecular Chaperone that Rescues Proteins from an Aggregated State
Molecular chaperones assist protein folding by facilitating their "forward" folding and preventing aggregation. However, once aggregates have formed, these chaperones cannot facilitate protein… Expand
Cofilin Changes the Twist of F-Actin: Implications for Actin Filament Dynamics and Cellular Function
Cofilin is an actin depolymerizing protein found widely distributed in animals and plants. We have used electron cryomicroscopy and helical reconstruction to identify its binding site on actin… Expand
EMDataBank.org: unified data resource for CryoEM
We introduce the Unified Data Resource for CryoEM, a global ‘one-stop shop’ resource for deposition and retrieval of cryoEM maps, models and associated metadata. Expand
Protein structure fitting and refinement guided by cryo-EM density.
- M. Topf, Keren Lasker, Ben M. Webb, H. Wolfson, W. Chiu, A. Sali
- Chemistry, Medicine
- 12 February 2008
For many macromolecular assemblies, both a cryo-electron microscopy map and atomic structures of its component proteins are available. Here we describe a method for fitting and refining a component… Expand
Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions
- W. Jiang, Z. Li, Z. Zhang, M. Baker, P. Prevelige, W. Chiu
- Biology, Medicine
- Nature Structural Biology
- 1 February 2003
Bacteriophage P22 is a prototypical biological machine used for studying protein complex assembly and capsid maturation. Using cryo-EM, we solved the structures of P22 before and after the capsid… Expand
Structure of the AcrAB-TolC multidrug efflux pump
The capacity of numerous bacterial species to tolerate antibiotics and other toxic compounds arises in part from the activity of energy-dependent transporters. In Gram-negative bacteria, many of… Expand
Quantitative analysis of cryo-EM density map segmentation by watershed and scale-space filtering, and fitting of structures by alignment to regions.
- G. Pintilie, Junjie Zhang, Thomas D. Goddard, W. Chiu, David C. Gossard
- Biology, Medicine
- Journal of structural biology
- 1 March 2010
Cryo-electron microscopy produces 3D density maps of molecular machines, which consist of various molecular components such as proteins and RNA. Segmentation of individual components in such maps is… Expand
Outcome of the First Electron Microscopy Validation Task Force Meeting
This Meeting Review describes the proceedings and conclusions from the inaugural meeting of the Electron Microscopy Validation Task Force organized by the Unified Data Resource for 3DEM… Expand
Seeing GroEL at 6 A resolution by single particle electron cryomicroscopy.
We present a reconstruction of native GroEL by electron cryomicroscopy (cryo-EM) and single particle analysis at 6 A resolution. alpha helices are clearly visible and beta sheet density is also… Expand
The pore structure of the closed RyR1 channel.
Using single particle electron cryomicroscopy, several helices in the membrane-spanning region of RyR1, including an inner transmembrane helix, a short pore helix, and a helix parallel to the… Expand