<?xml version="1.0" encoding="UTF-8"?>
<emdEntry accessCode="3127" version="1.9.6">
    <admin>
        <lastUpdate>2017-02-01</lastUpdate>
    </admin>
    <deposition>
        <status prior="REL">OBS</status>
        <depositionDate>2015-08-13</depositionDate>
        <depositionSite>PDBe</depositionSite>
        <processingSite>PDBe</processingSite>
        <headerReleaseDate>2015-09-16</headerReleaseDate>
        <mapReleaseDate>2017-02-01</mapReleaseDate>
        <obsoletedDate>2017-02-01</obsoletedDate>
        <details>Data reprocessed</details>
        <title>Structure of a cross-beta amyloid fibril from IGSNVVTWYQQL peptide of AL-DIA immunoglobulin light chain by cryo-EM and fiber diffraction</title>
        <authors>Schmidt A, Annamalai K, Schmidt M, Grigorieff N, Fandrich M</authors>
        <keywords>AL amyloidosis, cryo electron microscopy, steric zipper, three dimensional reconstruction</keywords>
        <primaryReference published="false">
            <journalArticle>
                <authors>Schmidt A, Annamalai K, Schmidt M, Grigorieff N, Fandrich M</authors>
                <articleTitle>Structural hierarchy, polymorphism and zipper-like packing of amyloid fibrils from an immunoglobulin light chain fragment</articleTitle>
                <journal>To Be Published</journal>
                <volume/>
                <firstPage/>
                <lastPage/>
                <year/>
            </journalArticle>
        </primaryReference>
    </deposition>
    <map>
        <file format="CCP4" sizeKb="142" type="map">emd_3127.map.gz</file>
        <dataType>Image stored as Reals</dataType>
        <dimensions>
            <numColumns>30</numColumns>
            <numRows>30</numRows>
            <numSections>40</numSections>
        </dimensions>
        <origin>
            <originCol>-15</originCol>
            <originRow>-15</originRow>
            <originSec>-20</originSec>
        </origin>
        <limit>
            <limitCol>14</limitCol>
            <limitRow>14</limitRow>
            <limitSec>19</limitSec>
        </limit>
        <spacing>
            <spacingCol>30</spacingCol>
            <spacingRow>30</spacingRow>
            <spacingSec>40</spacingSec>
        </spacing>
        <cell>
            <cellA units="A">253.19998</cellA>
            <cellB units="A">253.19998</cellB>
            <cellC units="A">337.59998</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>-2020.42968750</minimum>
            <maximum>8514.20019531</maximum>
            <average>695.82000732</average>
            <std>2629.44335938</std>
        </statistics>
        <spaceGroupNumber>1</spaceGroupNumber>
        <details>::::EMDATABANK.org::::EMD-3127::::</details>
        <pixelSpacing>
            <pixelX units="A">8.44</pixelX>
            <pixelY units="A">8.44</pixelY>
            <pixelZ units="A">8.44</pixelZ>
        </pixelSpacing>
        <contourLevel source="author">0.48</contourLevel>
        <annotationDetails>Reconstruction morphology 2 of a left handed amyloid-like fibril of the IGSNVVTWYQQL fragment of an immunoglobulin light chain</annotationDetails>
    </map>
    <supplement>
        <maskSet/>
        <sliceSet/>
        <figureSet>
            <figure>
                <file>emd_3127.png</file>
            </figure>
        </figureSet>
        <fscSet>
            <fsc>
                <file>emd_3127_fsc.xml</file>
            </fsc>
        </fscSet>
    </supplement>
    <sample>
        <numComponents>1</numComponents>
        <name>Amyloidogenic Fragment IGSNVVTWYQQL of Immunoglobulin Light Chain of Human AL Patient</name>
        <details>The sample forms long amyloid-like fibrils.</details>
        <sampleComponentList>
            <sampleComponent componentID="1">
                <entry>protein</entry>
                <sciName>Immunoglobulin Light Chain</sciName>
                <protein>
                    <sciSpeciesName ncbiTaxId="9606">Homo sapiens</sciSpeciesName>
                    <recombinantExpFlag>false</recombinantExpFlag>
                    <synSpeciesName>Human</synSpeciesName>
                    <externalReferences/>
                    <natSource>
                        <cell>Plasma cell</cell>
                        <organOrTissue>Blood</organOrTissue>
                        <cellLocation>extracellular</cellLocation>
                    </natSource>
                    <engSource/>
                </protein>
            </sampleComponent>
        </sampleComponentList>
    </sample>
    <experiment>
        <vitrification>
            <method>Incubation of 0.014 mg/ml fibril solution on glow discharged holey carbon grid for 30 seconds and backside blotting for 4 seconds before plunging.</method>
            <cryogenName>ETHANE</cryogenName>
            <humidity>50</humidity>
            <instrument>GATAN CRYOPLUNGE 3</instrument>
            <temperature units="Kelvin">100</temperature>
        </vitrification>
        <imaging>
            <electronSource>FIELD EMISSION GUN</electronSource>
            <electronDose units="e/A**2">25</electronDose>
            <imagingMode>BRIGHT FIELD</imagingMode>
            <nominalDefocusMin units="nm">1000</nominalDefocusMin>
            <nominalDefocusMax units="nm">5000</nominalDefocusMax>
            <illuminationMode>FLOOD BEAM</illuminationMode>
            <detector>FEI FALCON I (4k x 4k)</detector>
            <nominalCs units="mm">2.0</nominalCs>
            <calibratedMagnification>66350.7</calibratedMagnification>
            <temperature units="Kelvin">100</temperature>
            <microscope>FEI TECNAI F20</microscope>
            <date>12-NOV-2012</date>
            <specimenHolderModel>GATAN LIQUID NITROGEN</specimenHolderModel>
            <acceleratingVoltage units="kV">200</acceleratingVoltage>
            <nominalMagnification>50000</nominalMagnification>
        </imaging>
        <imageAcquisition>
            <numDigitalImages>5</numDigitalImages>
            <quantBitNumber>16</quantBitNumber>
        </imageAcquisition>
        <fitting/>
        <specimenPreparation>
            <helicalParameters>
                <deltaZ units="A">4.69</deltaZ>
                <deltaPhi units="degrees">0.824</deltaPhi>
                <axialSymmetry>C2</axialSymmetry>
                <hand>LEFT HANDED</hand>
            </helicalParameters>
            <specimenState>filament</specimenState>
            <specimenConc units="mg/ml">5.0</specimenConc>
            <specimenSupportDetails>C-flat 1.2/1.3-2C 400 mesh grids,
glow discharged</specimenSupportDetails>
            <buffer>
                <ph>8.0</ph>
                <details>50mM Tris-HCL</details>
            </buffer>
        </specimenPreparation>
    </experiment>
    <processing>
        <method>helical</method>
        <reconstruction>
            <algorithm>Projection matching and Fourier inversion</algorithm>
            <software>Frealix</software>
            <ctfCorrection>Defocus estimated for each helical subunit</ctfCorrection>
            <details>Final map was calculated from five single fibril reconstructions.</details>
            <resolutionByAuthor>28.5</resolutionByAuthor>
            <resolutionMethod>FSC 0.143, semi-independent</resolutionMethod>
        </reconstruction>
        <helical/>
    </processing>
</emdEntry>
