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    - PDB-2x31: Modelling of the complex between subunits BchI and BchD of magnes... -

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    Basic information

    Entry
    Database: PDB / ID: 2x31
    TitleModelling of the complex between subunits BchI and BchD of magnesium chelatase based on single-particle cryo-EM reconstruction at 7.5 ang
    DescriptorMAGNESIUM-CHELATASE 60 KDA SUBUNIT (E.C.6.6.1.1)
    MAGNESIUM-CHELATASE 38 KDA SUBUNIT (E.C.6.6.1.1)
    KeywordsLIGASE / BACTERIOCHLOROPHYLL BIOSYNTHESIS / PHOTOSYNTHESIS
    Specimen sourceRhodobacter capsulatus / archaea
    MethodElectron microscopy (7.5 A resolution / Single particle / Vitreous ice)
    AuthorsLunqvist, J. / Elmlund, H. / Peterson Wulff, R. / Berglund, L. / Elmlund, D. / Emanuelsson, C. / Hebert, H. / Willows, R.D. / Hansson, M. / Lindahl, M. / Al-Karadaghi, S.
    CitationStructure, 2010, 18, 354-365

    Structure, 2010, 18, 354-365 StrPapers
    ATP-induced conformational dynamics in the AAA+ motor unit of magnesium chelatase.
    Joakim Lundqvist / Hans Elmlund / Ragna Peterson Wulff / Lisa Berglund / Dominika Elmlund / Cecilia Emanuelsson / Hans Hebert / Robert D Willows / Mats Hansson / Martin Lindahl / Salam Al-Karadaghi

    DateDeposition: Jan 19, 2010 / Release: Nov 10, 2010 / Last modification: Mar 20, 2013

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    Assembly

    Deposited unit
    A: MAGNESIUM-CHELATASE 60 KDA SUBUNIT
    B: MAGNESIUM-CHELATASE 60 KDA SUBUNIT
    C: MAGNESIUM-CHELATASE 60 KDA SUBUNIT
    D: MAGNESIUM-CHELATASE 60 KDA SUBUNIT
    E: MAGNESIUM-CHELATASE 60 KDA SUBUNIT
    F: MAGNESIUM-CHELATASE 60 KDA SUBUNIT
    G: MAGNESIUM-CHELATASE 38 KDA SUBUNIT
    H: MAGNESIUM-CHELATASE 38 KDA SUBUNIT
    I: MAGNESIUM-CHELATASE 38 KDA SUBUNIT
    J: MAGNESIUM-CHELATASE 38 KDA SUBUNIT
    K: MAGNESIUM-CHELATASE 38 KDA SUBUNIT
    L: MAGNESIUM-CHELATASE 38 KDA SUBUNIT

    346 kDa, 12 molecules
    Theoretical massNumber of molelcules
    Total
    (without water)
    345,68112
    Polyers345,68112
    Non-polymers00
    Water0

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    #1idetical with deposited unit / defined by software (PISA) / Symmetry operations: (identity)x1
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    Components

    #1polypeptide(L) / MAGNESIUM-CHELATASE 60 KDA SUBUNIT / MG-PROTOPORPHYRIN IX CHELATASE, MG-CHELATASE SUBUNIT D / Fragment: RESIDUES 373-561 / Source: RHODOBACTER CAPSULATUS (gene. exp.) / References: UniProt: P26175, EC: 6.6.1.1
    #2polypeptide(L) / MAGNESIUM-CHELATASE 38 KDA SUBUNIT / MG-PROTOPORPHYRIN IX CHELATASE / Source: RHODOBACTER CAPSULATUS (gene. exp.) / References: UniProt: P26239, EC: 6.6.1.1

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    Experimental details

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    Experiment

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

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    Sample preparation

    Assembly of specimenName: BCHID COMPLEX OF RHODOBACTER CAPSULATUS MG CHELATASE / Aggregation state: PARTICLE
    Sample preparationpH: 8 / Sample conc.: 0.1 mg/ml
    Specimen supportDetails: HOLEY CARBON
    VitrificationDetails: LIQUID ETHANE

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    Electron microscopy imaging

    MicroscopyMicroscope model: JEOL 2010F
    Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 120 kV
    Electron lensMode: BRIGHT FIELD / Nominal magnification: 60000 X / Nominal defocus max: 5.5 nm / Nominal defocus min: 1 nm / Cs: 2 mm
    EM image scansNumber digital images: 18
    Radiation wavelengthRelative weight: 1

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    Processing

    3D reconstructionResolution: 7.5 A
    Least-squares processHighest resolution: 7.5 A
    Refine hist #LASTHighest resolution: 7.5 A
    Number of atoms included #LASTProtein: 22890 / Nucleic acid: 0 / Ligand: 0 / Solvent: 0 / Total: 22890

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