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    - PDB-3lue: Model of alpha-actinin CH1 bound to F-actin -

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    Basic information

    Entry
    Database: PDB / ID: 3lue
    TitleModel of alpha-actinin CH1 bound to F-actin
    DescriptorActin
    cytoplasmic 1
    Alpha-actinin-3
    KeywordsSTRUCTURAL PROTEIN / calponin homology domains / ATP-binding / Cytoskeleton / Methylation / Nucleotide-binding / Phosphoprotein / Actin-binding / Deafness / Disease mutation / Dystonia
    Specimen sourceHomo sapiens / human
    MethodElectron microscopy (15 A resolution / Helical / Vitreous ice (cryo EM))
    AuthorsGalkin, V.E. / Orlova, A. / Salmazo, A. / Djinovic-Carugo, K. / Egelman, E.H.
    CitationNat. Struct. Mol. Biol., 2010, 17, 614-616

    Nat. Struct. Mol. Biol., 2010, 17, 614-616 StrPapers
    Opening of tandem calponin homology domains regulates their affinity for F-actin.
    Vitold E Galkin / Albina Orlova / Anita Salmazo / Kristina Djinovic-Carugo / Edward H Egelman

    DateDeposition: Feb 17, 2010 / Release: Apr 28, 2010 / Last modification: May 19, 2010

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    Structure visualization

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    Assembly

    Deposited unit
    A: Actin, cytoplasmic 1
    B: Actin, cytoplasmic 1
    C: Actin, cytoplasmic 1
    D: Actin, cytoplasmic 1
    E: Actin, cytoplasmic 1
    F: Actin, cytoplasmic 1
    G: Actin, cytoplasmic 1
    H: Actin, cytoplasmic 1
    I: Actin, cytoplasmic 1
    J: Actin, cytoplasmic 1
    K: Alpha-actinin-3
    M: Alpha-actinin-3
    L: Alpha-actinin-3
    O: Alpha-actinin-3
    N: Alpha-actinin-3
    Q: Alpha-actinin-3
    P: Alpha-actinin-3
    S: Alpha-actinin-3
    R: Alpha-actinin-3
    T: Alpha-actinin-3

    541 kDa, 20 molecules
    Theoretical massNumber of molelcules
    Total
    (without water)
    541,23620
    Polyers541,23620
    Non-polymers00
    Water0

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

    #1polypeptide(L) / Actin, cytoplasmic 1 / Beta-actin, Actin, cytoplasmic 1, N-terminally processed / Source: Homo sapiens (gene. exp.) / References: UniProt: P60709
    #2polypeptide(L) / Alpha-actinin-3 / Alpha-actinin skeletal muscle isoform 3, F-actin cross-linking protein / Source: Homo sapiens (gene. exp.) / References: UniProt: Q08043

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    Experimental details

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    Experiment

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

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    Sample preparation

    Assembly of specimenName: F-actin decorated with alpha-actinin ABD (containing CH1 and CH2)
    Aggregation state: FILAMENT / Details: none / Composition: one to one binding / Number of components: 2
    ComponentName: F-actin / Type: PROTEIN / Ebi expression system: E. coli / Ebi tissue: muscle / Mutant flag: YES / Oligomeric details: helical polymer / Synonym: F-actin
    VitrificationCryogen name: ETHANE

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    Electron microscopy imaging

    EM imagingCamera length: 0 mm
    Electron gunAccelerating voltage: 200 kV / Illumination mode: FLOOD BEAM
    Electron lensMode: BRIGHT FIELD / Nominal magnification: 50000 X
    Specimen holderSpecimen holder model: GATAN LIQUID NITROGEN / Specimen holder type: gatan 626 / Tilt angle max: 0 deg. / Tilt angle min: 0 deg.
    CameraType: Kodak SO163
    EM image scansSampling size: 12.7 microns / Scanner model: NIKON COOLSCAN
    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: Chimera
    EM helical entityAngular rotation per subunit: 166.8 deg. / Axial rise per subunit: 27.7 A
    3D reconstructionMethod: back projection / Software: IHRSR / Resolution: 15 A / Resolution method: FSC at 0.5 / Nominal pixel size: 2.38 A/pix / Actual pixel size: 2.38 A/pix / CTF correction method: Weiner filter
    Details: AUTHORS STATE THAT THE STRANGE C-N BONDS WERE THE RESULT OF BREAKING THE CHAINS AT THESE POINTS TO DO RIGID BODY FITTING OF THE SUBDOMAINS.
    Atomic model buildingMethod: both manually and with Chimera / Software name: Chimera
    Details: AUTHORS STATE THAT THE STRANGE C-N BONDS WERE THE RESULT OF BREAKING THE CHAINS AT THESE POINTS TO DO RIGID BODY FITTING OF THE SUBDOMAINS.
    Ref space: REAL
    Number of atoms included #LASTProtein: 37910 / Nucleic acid: 0 / Ligand: 0 / Solvent: 0 / Total: 37910

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