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    <admin>
        <lastUpdate>2013-01-23</lastUpdate>
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    <deposition>
        <status prior="HPUB">OBS</status>
        <depositionDate>2012-08-11</depositionDate>
        <depositionSite>PDBe</depositionSite>
        <processingSite>PDBe</processingSite>
        <headerReleaseDate>2012-10-03</headerReleaseDate>
        <obsoletedDate>2013-01-23</obsoletedDate>
        <supersededByList>
            <entry>EMD-5530</entry>
            <entry>EMD-5531</entry>
            <entry>EMD-5532</entry>
            <entry>EMD-5533</entry>
        </supersededByList>
        <details>Duplicate submission.</details>
        <title>Cryo electron microscopy of mhttQ51 + TRiC</title>
        <authors>Shahmoradian SH, Galaz JG, Schmid MF, Cong Y, Khant HA, Spiess C, Frydman J, Ludtke SJ, Chiu W</authors>
        <keywords>Structural classification</keywords>
        <primaryReference published="false">
            <journalArticle>
                <authors>Shahmoradian SH, Galaz JG, Schmid MF, Cong Y, Khant HA, Spiess C, Frydman J, Ludtke SJ, Chiu W</authors>
                <articleTitle>Structural Basis for Inhibition of Huntingtin Aggregation by Chaperonin TRiC</articleTitle>
                <journal>To Be Published</journal>
                <volume/>
                <firstPage/>
                <lastPage/>
                <year/>
            </journalArticle>
        </primaryReference>
    </deposition>
    <map>
        <file format="CCP4" sizeKb="3457" type="map">emd_2178.map.gz</file>
        <dataType>Image stored as Reals</dataType>
        <dimensions>
            <numColumns>96</numColumns>
            <numRows>96</numRows>
            <numSections>96</numSections>
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        <origin>
            <originCol>0</originCol>
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        <limit>
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        <spacing>
            <spacingCol>96</spacingCol>
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            <spacingSec>96</spacingSec>
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        <cell>
            <cellA units="A">422.496</cellA>
            <cellB units="A">422.496</cellB>
            <cellC units="A">422.496</cellC>
            <cellAlpha units="degrees">90.0</cellAlpha>
            <cellBeta units="degrees">90.0</cellBeta>
            <cellGamma units="degrees">90.0</cellGamma>
        </cell>
        <axisOrder>
            <axisOrderFast>X</axisOrderFast>
            <axisOrderMedium>Y</axisOrderMedium>
            <axisOrderSlow>Z</axisOrderSlow>
        </axisOrder>
        <statistics>
            <minimum>-3.28584862</minimum>
            <maximum>6.44397163</maximum>
            <average>0.00142521</average>
            <std>0.72210234</std>
        </statistics>
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        <details>::::EMDATABANK.org::::EMD-2178::::</details>
        <pixelSpacing>
            <pixelX units="A">4.401</pixelX>
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            <pixelZ units="A">4.401</pixelZ>
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        <contourLevel source="author">3.0</contourLevel>
        <annotationDetails>Bias-free reconstruction of apo-TRiC from subtomograms of mutant huntingtin incubated with TRiC</annotationDetails>
    </map>
    <supplement>
        <maskSet/>
        <sliceSet/>
        <figureSet/>
        <fscSet/>
    </supplement>
    <sample>
        <numComponents>2</numComponents>
        <name>TRiC plus mhttQ51</name>
        <sampleComponentList>
            <sampleComponent componentID="1">
                <entry>protein</entry>
                <sciName>Tcp Ring Complex</sciName>
                <protein>
                    <sciSpeciesName ncbiTaxId="92907">Cirsium vulgare</sciSpeciesName>
                    <recombinantExpFlag>true</recombinantExpFlag>
                    <externalReferences/>
                    <natSource/>
                    <engSource/>
                </protein>
            </sampleComponent>
            <sampleComponent componentID="2">
                <entry>protein</entry>
                <sciName>mutant huntingtin Q51 exon 1 fragment</sciName>
                <protein>
                    <recombinantExpFlag>true</recombinantExpFlag>
                    <sciSpeciesName ncbiTaxId="92907">Cirsium vulgare</sciSpeciesName>
                    <externalReferences/>
                    <natSource/>
                    <engSource/>
                </protein>
            </sampleComponent>
        </sampleComponentList>
    </sample>
    <experiment>
        <vitrification>
            <cryogenName>NITROGEN</cryogenName>
            <instrument>FEI VITROBOT MARK III</instrument>
        </vitrification>
        <imaging>
            <electronSource>LAB6</electronSource>
            <electronDose units="e/A**2">62</electronDose>
            <imagingMode>BRIGHT FIELD</imagingMode>
            <illuminationMode>FLOOD BEAM</illuminationMode>
            <microscope>JEOL 2100</microscope>
            <date>19-MAR-2009</date>
            <specimenHolderModel>GATAN LIQUID NITROGEN</specimenHolderModel>
            <acceleratingVoltage units="kV">200</acceleratingVoltage>
        </imaging>
        <imageAcquisition/>
        <fitting/>
        <specimenPreparation/>
    </experiment>
    <processing>
        <method>subtomogramAveraging</method>
        <reconstruction>
            <software>IMOD, EMAN2</software>
            <resolutionByAuthor>44</resolutionByAuthor>
            <resolutionMethod>FSC 0.143</resolutionMethod>
        </reconstruction>
        <subtomogramAveraging>
            <details>Average number of tilts used in the 3D reconstructions: 60. Average tomographic tilt angle increment: 2.</details>
        </subtomogramAveraging>
    </processing>
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