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    - PDB-3ktt: Atomic model of bovine TRiC CCT2(beta) subunit derived from a 4.0... -

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    Basic information

    Entry
    Database: PDB / ID: 3ktt
    TitleAtomic model of bovine TRiC CCT2(beta) subunit derived from a 4.0 Angstrom cryo-EM map
    DescriptorT-complex protein 1 subunit beta
    KeywordsCHAPERONE / TRiC/CCT / CCT2(beta) / cryo-EM / ATP-binding / Chaperone / Nucleotide-binding
    Specimen sourceBos taurus / mammal / bovine /
    MethodElectron microscopy (4 A resolution / Single particle / Vitreous ice (cryo EM))
    AuthorsCong, Y. / Baker, M.L. / Ludtke, S.J. / Frydman, J. / Chiu, W.
    CitationProc. Natl. Acad. Sci. U.S.A., 2010, 107, 4967-4972

    primary. Proc. Natl. Acad. Sci. U.S.A., 2010, 107, 4967-4972 StrPapers
    4.0-A resolution cryo-EM structure of the mammalian chaperonin TRiC/CCT reveals its unique subunit arrangement.
    Yao Cong / Matthew L Baker / Joanita Jakana / David Woolford / Erik J Miller / Stefanie Reissmann / Ramya N Kumar / Alyssa M Redding-Johanson / Tanveer S Batth / Aindrila Mukhopadhyay / Steven J Ludtke / Judith Frydman / Wah Chiu

    #1. To be Published Search PubMed
    To be published
    Cong, Y. / Baker, M.L. / Jakana, J. / Woolford, D. / Miller, E.J. / Reissmann, S. / Kumar, R.N. / Redding-Johanson, A.M. / Batth, T.S. / Mukhopadhyay, A. / Ludtke, S.J. / Frydman, J. / Chiu, W.

    DateDeposition: Nov 25, 2009 / Release: Mar 16, 2010 / Last modification: Apr 7, 2010

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    Assembly

    Deposited unit
    B: T-complex protein 1 subunit beta

    55.1 kDa, 1 molecules
    Theoretical massNumber of molelcules
    Total
    (without water)
    55,1081
    Polyers55,1081
    Non-polymers00
    Water0

    Omokage search
    #1idetical with deposited unit / defined by author / Symmetry operations: (identity)x1
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    Components

    #1polypeptide(L) / T-complex protein 1 subunit beta / TCP-1-beta, CCT-beta / Source: Bos taurus (gene. exp.) / References: UniProt: Q3ZBH0

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    Experimental details

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    Experiment

    ExperimentMethod: ELECTRON MICROSCOPY
    EM experimentReconstruction method: SINGLE PARTICLE / Specimen type: VITREOUS ICE (CRYO EM)

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    Sample preparation

    Assembly of specimenName: CCT2(beta) subunit in the both-ring closed bovine TRiC complex
    Aggregation state: PARTICLE
    VitrificationDetails: vitrification using ethane as cryogen

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    Electron microscopy imaging

    MicroscopyMicroscope model: JEM3200FSC / Date: 2007-08 ~ 2008-08
    Electron gunElectron source: Field Emission Gun / Accelerating voltage: 300 kV
    Electron lensNominal magnification: 50000 X / Nominal defocus max: 3000 nm / Nominal defocus min: 1000 nm / Cs: 4.1 mm
    Specimen holderTemperature: 101 K / Tilt angle max: 0 deg. / Tilt angle min: 0 deg.
    CameraType: Kodak SO163 film
    RadiationDiffraction protocol: SINGLE WAVELENGTH / Monochromatic or laue m l: M / Scattering type: x-ray
    Radiation wavelengthRelative weight: 1

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    Processing

    Image selectionSoftware name: COOT, Chimera, Modeller
    3D reconstructionMethod: Projection matching / Resolution: 4 A / Actual pixel size: 1.2 A/pix / CTF correction method: FSC at 0.5 cut-off
    Details: Single particle 3D reconstruction using EMAN1.8+ with our recently developed 2-D fast rotation matching method (FRM2D) for the image alignment.
    Atomic model buildingMethod: Local refinement, Flexible fitting / Software name: COOT, Chimera, Modeller / Ref protocol: Local refinement, Flexible fitting / Ref space: REAL
    Number of atoms included #LASTProtein: 3855 / Nucleic acid: 0 / Ligand: 0 / Solvent: 0 / Total: 3855

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