<emdEntry accessCode="6727" version="1.9.6" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="https://github.com/emdb-empiar/emdb-schemas/tree/master/current/emdb.xsd">
    <admin>
        <lastUpdate>2018-08-22</lastUpdate>
    </admin>
    <deposition>
        <status>REL</status>
        <depositionDate>2017-05-10</depositionDate>
        <depositionSite>PDBj</depositionSite>
        <processingSite>PDBj</processingSite>
        <headerReleaseDate>2018-06-13</headerReleaseDate>
        <mapReleaseDate>2018-06-13</mapReleaseDate>
        <title>Folding intermediate of RuBisCO in complex with the GroEL chaperonin. Class3.</title>
        <authors>Natesh R, Clare DK, Farr GW, Horwich AL, Saibil HR</authors>
        <primaryReference published="true">
            <journalArticle>
                <authors>Natesh R, Clare DK, Farr GW, Horwich AL, Saibil HR</authors>
                <articleTitle>A two-domain folding intermediate of RuBisCO in complex with the GroEL chaperonin.</articleTitle>
                <journal>Int. J. Biol. Macromol.</journal>
                <volume>118</volume>
                <firstPage>671</firstPage>
                <lastPage>675</lastPage>
                <year>2018</year>
                <externalReference type="pubmed">29959019</externalReference>
                <externalReference type="doi">doi:10.1016/j.ijbiomac.2018.06.120</externalReference>
                <externalReference type="issn">1879-0003</externalReference>
                <externalReference type="csd">0708</externalReference>
                <externalReference type="astm">IJBMDR</externalReference>
            </journalArticle>
        </primaryReference>
    </deposition>
    <map>
        <file format="CCP4" sizeKb="30119" type="map">emd_6727.map.gz</file>
        <dataType>Image stored as Reals</dataType>
        <dimensions>
            <numRows>196</numRows>
            <numColumns>196</numColumns>
            <numSections>196</numSections>
        </dimensions>
        <origin>
            <originRow>0.</originRow>
            <originCol>0.</originCol>
            <originSec>0.</originSec>
        </origin>
        <limit>
            <limitRow>195.</limitRow>
            <limitCol>195.</limitCol>
            <limitSec>195.</limitSec>
        </limit>
        <spacing>
            <spacingRow>196</spacingRow>
            <spacingCol>196</spacingCol>
            <spacingSec>196</spacingSec>
        </spacing>
        <cell>
            <cellA units="A">548.8</cellA>
            <cellB units="A">548.8</cellB>
            <cellC units="A">548.8</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>-0.70907927</minimum>
            <maximum>9.996134</maximum>
            <average>0.016255789</average>
            <std>0.23185983</std>
        </statistics>
        <spaceGroupNumber>1</spaceGroupNumber>
        <details />
        <pixelSpacing>
            <pixelX units="A">2.8</pixelX>
            <pixelY units="A">2.8</pixelY>
            <pixelZ units="A">2.8</pixelZ>
        </pixelSpacing>
        <contourLevel source="author">0.25</contourLevel>
        <annotationDetails>Folding intermediate of RuBisCO in complex with the GroEL chaperonin.  Class3.</annotationDetails>
    </map>
    <sample>
        <numComponents>2</numComponents>
        <name>Non-native RuBisCO in complex with chaperonin GroEL</name>
        <details>Apo GroEL.D473C.His6 with unbound RuBisCO folding intermediate as seen in 3D reconstruction for Class3.  Only GroEL region was observed in EM map.</details>
        <sampleComponentList>
            <sampleComponent componentID="1">
                <entry>protein</entry>
                <sciName>Non-native RuBisCO in complex with chaperonin GroEL</sciName>
                <molWtTheo units="MDa">0.812</molWtTheo>
                <details>Apo GroEL.D473C.His6 with unbound RuBisCO folding intermediate as seen in 3D reconstruction for Class3.  Only GroEL region was observed in EM map.</details>
                <protein>
                    <sciSpeciesName ncbiTaxId="562">Escherichia coli</sciSpeciesName>
                    <recombinantExpFlag>false</recombinantExpFlag>
                    <natSource />
                    <engSource>
                        <expSystem ncbiTaxId="562">Escherichia coli</expSystem>
                    </engSource>
                </protein>
            </sampleComponent>
            <sampleComponent componentID="2">
                <entry>protein</entry>
                <sciName>GroEL</sciName>
                <details>GroEL.D473C.His6  Tetradecamer</details>
                <protein>
                    <sciSpeciesName ncbiTaxId="562">Escherichia coli</sciSpeciesName>
                    <recombinantExpFlag>false</recombinantExpFlag>
                    <natSource />
                    <engSource>
                        <expSystem ncbiTaxId="562">Escherichia coli</expSystem>
                    </engSource>
                </protein>
            </sampleComponent>
        </sampleComponentList>
    </sample>
    <experiment>
        <vitrification>
            <cryogenName>ETHANE</cryogenName>
            <temperature units="Kelvin">298</temperature>
            <instrument>HOMEMADE PLUNGER</instrument>
            <details>Blot  approx. 1 sec before plunging.  Visual.. </details>
        </vitrification>
        <imaging>
            <electronSource>FIELD EMISSION GUN</electronSource>
            <electronDose units="e/A**2">10.0</electronDose>
            <imagingMode>BRIGHT FIELD</imagingMode>
            <nominalDefocusMin units="nm">1000.0</nominalDefocusMin>
            <nominalDefocusMax units="nm">3500.0</nominalDefocusMax>
            <illuminationMode>FLOOD BEAM</illuminationMode>
            <detector>KODAK SO-163 FILM</detector>
            <nominalCs units="mm">2.0</nominalCs>
            <calibratedMagnification>50000.</calibratedMagnification>
            <temperatureMin units="Kelvin">100.0</temperatureMin>
            <temperatureMax units="Kelvin">100.0</temperatureMax>
            <microscope>FEI TECNAI F20</microscope>
            <specimenHolderModel>GATAN LIQUID NITROGEN</specimenHolderModel>
            <acceleratingVoltage units="kV">200</acceleratingVoltage>
            <nominalMagnification>50000.</nominalMagnification>
        </imaging>
        <imageAcquisition>
            <numDigitalImages>468</numDigitalImages>
            <samplingSize units="microns">7.0</samplingSize>
            <details>Images were collected on Kodak SO-163 Film.  Dose was 10-15 e-/A2/sec.</details>
        </imageAcquisition>
        <fitting>
            <pdbEntryIdList>
                <pdbEntryId>1OEL</pdbEntryId>
            </pdbEntryIdList>
            <refProtocol>rigid body</refProtocol>
            <details>Rigid body fit</details>
        </fitting>
        <specimenPreparation>
            <specimenState>particle</specimenState>
            <specimenConc units="mg/ml">0.0863</specimenConc>
            <buffer>
                <ph>7.5</ph>
                <details>Folding Buffer (FB) consists of 50 mM HEPES pH7.5, 10 mM KOAc, 10 mM Mg(OAc)2, 10 mM DTT.

RuBisCO denatured in 20mM HCl, 10 M Urea, 20 mM DTT</details>
            </buffer>
            <specimenSupportDetails>The C-flat holey grids were coated with thin home made carbon film.</specimenSupportDetails>
        </specimenPreparation>
    </experiment>
    <processing>
        <method>singleParticle</method>
        <reconstruction>
            <algorithm>BACK PROJECTION</algorithm>
            <ctfCorrection>CTF phase flipping was perfomed</ctfCorrection>
            <resolutionByAuthor>11.0</resolutionByAuthor>
            <resolutionMethod>FSC 0.5 CUT-OFF</resolutionMethod>
            <details>In 3D reconstruction for Class 3:   Resolution is 9 A  for C7 symmetrised map  after iteration cycle 7.   Resolution is 11 A for asymmetric C1 reconstruction after iteration cycle 13.</details>
        </reconstruction>
        <singleParticle>
            <appliedSymmetry>C1</appliedSymmetry>
            <numProjections>6003</numProjections>
            <details>For the binary complex data sets, the positions of particles were noted in MRC programme XIMDISP. Perl script was used to extract particles in boxes of 512 x 512 pixels using the MRC program LABEL, and phase corrected using SPIDER. After CTF correction, the box size was cropped and sampling reduced so that all images were at 2.8 A per pixel in 196 x 196 pixel boxes. Images were band-pass filtered between 285 A and 6 A and normalized to zero mean and the same sigma in SPIDER.</details>
        </singleParticle>
    </processing>
</emdEntry>