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<emd emdb_id="EMD-2178" version="3.0.1.9">
    <admin>
        <status_history_list>
            <status status_id="1">
                <code>HPUB</code>
            </status>
        </status_history_list>
        <current_status>
            <code superseded="true">OBS</code>
            <processing_site>PDBe</processing_site>
        </current_status>
        <sites>
            <deposition>PDBe</deposition>
            <last_processing>PDBe</last_processing>
        </sites>
        <key_dates>
            <deposition>2012-08-11</deposition>
            <header_release>2012-10-03</header_release>
            <obsolete>2013-01-23</obsolete>
            <update>2013-01-23</update>
        </key_dates>
        <superseded_by_list>
            <entry>
                <entry>EMD-5530</entry>
            </entry>
            <entry>
                <entry>EMD-5531</entry>
            </entry>
            <entry>
                <entry>EMD-5532</entry>
            </entry>
            <entry>
                <entry>EMD-5533</entry>
            </entry>
        </superseded_by_list>
        <title>Cryo electron microscopy of mhttQ51 + TRiC</title>
        <authors_list>
            <author>Shahmoradian SH</author>
            <author>Galaz JG</author>
            <author>Schmid MF</author>
            <author>Cong Y</author>
            <author>Khant HA</author>
            <author>Spiess C</author>
            <author>Frydman J</author>
            <author>Ludtke SJ</author>
            <author>Chiu W</author>
        </authors_list>
        <keywords>Structural classification</keywords>
    </admin>
    <crossreferences>
        <citation_list>
            <primary_citation>
                <journal_citation published="false">
                    <author order="1">Shahmoradian SH</author>
                    <author order="2">Galaz JG</author>
                    <author order="3">Schmid MF</author>
                    <author order="4">Cong Y</author>
                    <author order="5">Khant HA</author>
                    <author order="6">Spiess C</author>
                    <author order="7">Frydman J</author>
                    <author order="8">Ludtke SJ</author>
                    <author order="9">Chiu W</author>
                    <title>Structural Basis for Inhibition of Huntingtin Aggregation by Chaperonin TRiC</title>
                    <journal>To Be Published</journal>
                </journal_citation>
            </primary_citation>
        </citation_list>
    </crossreferences>
    <sample>
        <name>TRiC plus mhttQ51</name>
        <supramolecule_list>
            <sample_supramolecule supramolecule_id="1000">
                <name>TRiC plus mhttQ51</name>
                <number_unique_components>2</number_unique_components>
            </sample_supramolecule>
        </supramolecule_list>
        <macromolecule_list>
            <protein_or_peptide macromolecule_id="1">
                <name>Tcp Ring Complex</name>
                <natural_source database="NCBI">
                    <organism ncbi="92907">Cirsium vulgare</organism>
                </natural_source>
                <recombinant_exp_flag>true</recombinant_exp_flag>
                <recombinant_expression database="NCBI"/>
                <sequence/>
            </protein_or_peptide>
            <protein_or_peptide macromolecule_id="2">
                <name>mutant huntingtin Q51 exon 1 fragment</name>
                <natural_source database="NCBI">
                    <organism ncbi="92907">Cirsium vulgare</organism>
                </natural_source>
                <recombinant_exp_flag>true</recombinant_exp_flag>
                <recombinant_expression database="NCBI"/>
                <sequence/>
            </protein_or_peptide>
        </macromolecule_list>
    </sample>
    <structure_determination_list>
        <structure_determination structure_determination_id="1">
            <method>subtomogramAveraging</method>
            <specimen_preparation_list>
                <subtomogram_averaging_preparation preparation_id="1">
                    <vitrification>
                        <cryogen_name>NITROGEN</cryogen_name>
                        <instrument>FEI VITROBOT MARK III</instrument>
                    </vitrification>
                </subtomogram_averaging_preparation>
            </specimen_preparation_list>
            <microscopy_list>
                <subtomogram_averaging_microscopy microscopy_id="1">
                    <microscope>JEOL 2100</microscope>
                    <illumination_mode>FLOOD BEAM</illumination_mode>
                    <imaging_mode>BRIGHT FIELD</imaging_mode>
                    <electron_source>LAB6</electron_source>
                    <acceleration_voltage units="kV">200</acceleration_voltage>
                    <specimen_holder_model>GATAN LIQUID NITROGEN</specimen_holder_model>
                    <date>2009-03-19</date>
                    <image_recording_list>
                        <image_recording>
                            <average_electron_dose_per_image units="e/Å^2">62</average_electron_dose_per_image>
                        </image_recording>
                    </image_recording_list>
                    <tilt_series>
                        <axis1/>
                    </tilt_series>
                </subtomogram_averaging_microscopy>
            </microscopy_list>
            <subtomogram_averaging_processing image_processing_id="1">
                <details>Average number of tilts used in the 3D reconstructions: 60. Average tomographic tilt angle increment: 2.</details>
                <final_reconstruction>
                    <resolution units="Å" res_type="BY AUTHOR">44.0</resolution>
                    <resolution_method>FSC 0.143 CUT-OFF</resolution_method>
                    <software_list>
                        <software>
                            <name>IMOD, EMAN2</name>
                        </software>
                    </software_list>
                </final_reconstruction>
            </subtomogram_averaging_processing>
        </structure_determination>
    </structure_determination_list>
    <map format="CCP4" size_kbytes="3457">
        <file>emd_2178.map.gz</file>
        <symmetry>
            <space_group>1</space_group>
        </symmetry>
        <data_type>IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)</data_type>
        <dimensions>
            <col>96</col>
            <row>96</row>
            <sec>96</sec>
        </dimensions>
        <origin>
            <col>0</col>
            <row>0</row>
            <sec>0</sec>
        </origin>
        <spacing>
            <x>96</x>
            <y>96</y>
            <z>96</z>
        </spacing>
        <cell>
            <a units="Å">422.496</a>
            <b units="Å">422.496</b>
            <c units="Å">422.496</c>
            <alpha units="deg">90.0</alpha>
            <beta units="deg">90.0</beta>
            <gamma units="deg">90.0</gamma>
        </cell>
        <axis_order>
            <fast>X</fast>
            <medium>Y</medium>
            <slow>Z</slow>
        </axis_order>
        <statistics>
            <minimum>-3.28584862</minimum>
            <maximum>6.44397163</maximum>
            <average>0.00142521</average>
            <std>0.72210234</std>
        </statistics>
        <pixel_spacing>
            <x units="Å">4.401</x>
            <y units="Å">4.401</y>
            <z units="Å">4.401</z>
        </pixel_spacing>
        <contour_list>
            <contour primary="true">
                <level>3.0</level>
                <source>AUTHOR</source>
            </contour>
        </contour_list>
        <annotation_details>Bias-free reconstruction of apo-TRiC from subtomograms of mutant huntingtin incubated with TRiC</annotation_details>
        <details>::::EMDATABANK.org::::EMD-2178::::</details>
    </map>
</emd>
